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Search results 2301 to 2400 out of 4706 for Coil

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Type Details Score
Publication
11921392 | -
First Author: Frey M
Year: 2002
Journal: Chembiochem
Title: Hydrogenases: hydrogen-activating enzymes.
Volume: 3
Issue: 2-3
Pages: 153-60
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Publication
2661538 | -
First Author: Voordouw G
Year: 1989
Journal: J Bacteriol
Title: Organization of the genes encoding [Fe] hydrogenase in Desulfovibrio vulgaris subsp. oxamicus Monticello.
Volume: 171
Issue: 7
Pages: 3881-9
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Publication
9195887 | -
First Author: Mayans O
Year: 1997
Journal: Structure
Title: Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases.
Volume: 5
Issue: 5
Pages: 677-89
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Publication
25781180 | -
First Author: Ott C
Year: 2015
Journal: PLoS One
Title: Detailed analysis of the human mitochondrial contact site complex indicate a hierarchy of subunits.
Volume: 10
Issue: 3
Pages: e0120213
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Publication
17558409 | J:123018
First Author: Delous M
Year: 2007
Journal: Nat Genet
Title: The ciliary gene RPGRIP1L is mutated in cerebello-oculo-renal syndrome (Joubert syndrome type B) and Meckel syndrome.
Volume: 39
Issue: 7
Pages: 875-81
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Publication
8611682 | J:111170
First Author: van Vugt MJ
Year: 1996
Journal: Blood
Title: FcR gamma-chain is essential for both surface expression and function of human Fc gamma RI (CD64) in vivo.
Volume: 87
Issue: 9
Pages: 3593-9
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Publication
1714902 | -
First Author: Rodewald HR
Year: 1991
Journal: J Biol Chem
Title: The high affinity Fc epsilon receptor gamma subunit (Fc epsilon RI gamma) facilitates T cell receptor expression and antigen/major histocompatibility complex-driven signaling in the absence of CD3 zeta and CD3 eta.
Volume: 266
Issue: 24
Pages: 15974-8
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Publication
18760284 | -
First Author: Lamour V
Year: 2008
Journal: J Mol Biol
Title: Crystal structure of Escherichia coli Rnk, a new RNA polymerase-interacting protein.
Volume: 383
Issue: 2
Pages: 367-79
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Publication
19787265 | -
First Author: Abiatari I
Year: 2009
Journal: Int J Oncol
Title: The microtubule-associated protein MAPRE2 is involved in perineural invasion of pancreatic cancer cells.
Volume: 35
Issue: 5
Pages: 1111-6
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Publication
17658256 | J:127422
First Author: Straube A
Year: 2007
Journal: Curr Biol
Title: EB3 regulates microtubule dynamics at the cell cortex and is required for myoblast elongation and fusion.
Volume: 17
Issue: 15
Pages: 1318-25
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Publication
15788569 | J:100748
First Author: Chitu V
Year: 2005
Journal: Mol Biol Cell
Title: The PCH family member MAYP/PSTPIP2 directly regulates F-actin bundling and enhances filopodia formation and motility in macrophages.
Volume: 16
Issue: 6
Pages: 2947-59
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Publication
16397132 | J:125785
First Author: Grosse J
Year: 2006
Journal: Blood
Title: Mutation of mouse Mayp/Pstpip2 causes a macrophage autoinflammatory disease.
Volume: 107
Issue: 8
Pages: 3350-8
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Publication
16339905 | -
First Author: Roepman R
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: Interaction of nephrocystin-4 and RPGRIP1 is disrupted by nephronophthisis or Leber congenital amaurosis-associated mutations.
Volume: 102
Issue: 51
Pages: 18520-5
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Publication
26887924 | J:234739
 
First Author: Marei H
Year: 2016
Journal: Nat Commun
Title: Differential Rac1 signalling by guanine nucleotide exchange factors implicates FLII in regulating Rac1-driven cell migration.
Volume: 7
Pages: 10664
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Publication
24308970 | -
First Author: Boissier P
Year: 2014
Journal: Cell Signal
Title: The guanine nucleotide exchange factor Tiam1: a Janus-faced molecule in cellular signaling.
Volume: 26
Issue: 3
Pages: 483-91
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Protein Domain
IPR002049 | LE_dom
Type: Domain
Description: This entry represents the laminin-type EGF-like domain (LE) found in Laminin subunit gamma-1 and Netrin-1 from Homo sapiens and Mus musculus. Laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation [, ]. They are composed of distinct but related alpha, beta and gamma chains that form a cross-shaped molecule consisting of a long arm and three short globular arms. The long arm has a coiled coil structure contributed by all three chains and cross-linked by interchain disulphide bonds [, ]. Beside the different types of globular domains each subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines []. The tertiary structure of this domain is remotely similar in its N-terminal to that of the EGF-like module [, ](see ). The number of copies of the LE domain in the different forms of laminins is highly variable; from 3 up to 22 copies have been found.A schematic representation of the topology of the four disulphide bonds in the LE domain is shown below.+-------------------++-|-----------+ | +--------+ +-----------------+| | | | | | | |xxCxCxxxxxxxxxxxCxxxxxxxCxxCxxxxxGxxCxxCxxgaagxxxxxxxxxxxCxxsssssssssssssssssssssssssssssssssss'C': conserved cysteine involved in a disulphide bond'a': conserved aromatic residue'G': conserved glycine (lower case = less conserved)'s': region similar to the EGF-like domainLong consecutive arrays of LE domains in laminins form rod-like elements of limited flexibility [], which determine the spacing in the formation of laminin networks of basement membranes [].Netrins control guidance of the central nervous system commissural axons and peripheral motor axons [, , , ]. This protein also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis, thus being involved in tumorigenesis [, ].
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Protein Domain
IPR014831 | Hemagglutn_stalk_influenz-C
Type: Domain
Description: Haemagglutinin (HA) is one of two main surface fusion glycoproteins embedded in the envelope of influenza viruses, the other being neuraminidase (NA). There are sixteen known HA subtypes (H1-H16) and nine NA subtypes (N1-N9), which together are used to classify influenza viruses (e.g. H5N1). The antigenic variations in HA and NA enable the virus to evade host antibodies made to previous influenza strains, accounting for recurrent influenza epidemics []. The HA glycoprotein is present in the viral membrane as a single polypeptide (HA0), which must be cleaved by the host's trypsin-like proteases to produce two peptides (HA1 and HA2) in order for the virus to be infectious. Once HA0 is cleaved, the newly exposed N-terminal of the HA2 peptide then acts to fuse the viral envelope to the cellular membrane of the host cell, which allows the viral negative-stranded RNA to infect the host cell. The type of host protease can influence the infectivity and pathogenicity of the virus.The haemagglutinin glycoprotein is a trimer containing three structurally distinct regions: a globular head consisting of anti-parallel β-sheets that form a β-sandwich with a jelly-roll fold (contains the receptor binding site and the HA1/HA2 cleavage site); a triple-stranded, coiled-coil, α-helical stalk; and a globular foot composed of anti-parallel β-sheets [, ]. Each monomer consists of an intact HA0 polypeptide with the HA1 and HA2 regions linked by disulphide bonds. The N terminus of HA1 provides the central strand in the 5-stranded globular foot, while the rest of the HA1 chain makes its way to the 8-stranded globular head. HA2 provides two alpha helices, which form part of the triple-stranded coiled-coil that stabilises the trimer, its C terminus providing the remaining strands of the 5-stranded globular foot.This entry represents the stalk segment of haemagglutinin in influenza C virus. It forms a coiled coil structure [].
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Protein Domain
IPR008953 | Fe_hydrogenase_HydB
Type: Homologous_superfamily
Description: Many microorganisms, such as methanogenic, acetogenic, nitrogen-fixing, photosynthetic, or sulphate-reducing bacteria, metabolise hydrogen. Hydrogen activation is mediated by a family of enzymes, termed hydrogenases, which either provide these organisms with reducing power from hydrogen oxidation, or act as electron sinks. There are two hydrogenases families that differ functionally from each other: NiFe hydrogenases tend to be more involved in hydrogen oxidation, while Iron-only FeFe (Fe only) hydrogenases in hydrogen production. Fe only hydrogenases () show a common core structure, which contains a moiety, deeply buried inside the protein, with an Fe-Fe dinuclear centre, nonproteic bridging, terminal CO and CN- ligands attached to each of the iron atoms, and a dithio moiety, which also bridges the two iron atoms and has been tentatively assigned as a di(thiomethyl)amine. This common core also harbours three [4Fe-4S]iron-sulphur clusters []. In FeFe hydrogenases, as in NiFe hydrogenases, the set of iron-sulphur clusters is dispersed regularly between the dinuclear Fe-Fe centre and the molecular surface. These clusters are distant by about 1.2 nm from each other but the [4Fe-4S]cluster closest to the dinuclear centre is covalently bound to one of the iron atoms though a thiolate bridging ligand. The moiety including the dinuclear centre, the thiolate bridging ligand, and the proximal [4Fe-4S]cluster is known as the H-cluster. A channel, lined with hydrophobic amino acid side chains, nearly connects the dinuclear centre and the molecular surface. Furthermore hydrogen-bonded water molecule sites have been identified at the interior and at the surface of the protein.The small subunit is comprised of alternating random coil and alpha helical structures that encompass the large subunit in a novel protein fold [].The localisation of iron hydrogenases can be cytoplasmic or periplasmic. Periplasmic iron hydrogenases in Desulfovibrio consists of a large subunit (HydA) and a small subunit (HydB) [].
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Protein
Q8VCN9
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false
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Protein
Q8C7M8
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: false
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Protein
E9PZ67
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: true
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Protein
A0A0R4J0M1
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false
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Publication
10368269 | -
First Author: Nicolet Y
Year: 1999
Journal: Structure
Title: Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center.
Volume: 7
Issue: 1
Pages: 13-23
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Publication
9628486 | -
First Author: Wang S
Year: 1998
Journal: Nat Struct Biol
Title: Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum.
Volume: 5
Issue: 6
Pages: 476-83
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Publication
26234751 | J:223062
First Author: Palmer K
Year: 2016
Journal: Dev Biol
Title: Discovery and characterization of spontaneous mouse models of craniofacial dysmorphology.
Volume: 415
Issue: 2
Pages: 216-227
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Protein Coding Gene
MGI:894689 | Ywhae
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1270156 | Septin4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:108390 | Kif2a
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098268 | Kif5b
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2444304 | Vps13a
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2444576 | Kif20b
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:3036247 | Lmtk2
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
20562862 | J:161922
First Author: Tang T
Year: 2010
Journal: Nat Biotechnol
Title: A mouse knockout library for secreted and transmembrane proteins.
Volume: 28
Issue: 7
Pages: 749-55
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Publication
- | J:171883
     
First Author: Lexicon Genetics, Inc
Year: 2011
Journal: Database Download
Title: MGI download of Lexicon knockout data
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Publication
17459884 | J:123573
First Author: Terawaki S
Year: 2007
Journal: J Biol Chem
Title: Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex.
Volume: 282
Issue: 27
Pages: 19854-62
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Protein
Q3TY65
Organism: Mus musculus/domesticus
Length: 431  
Fragment?: false
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Publication
23798443 | J:198812
First Author: Wei Z
Year: 2013
Journal: Proc Natl Acad Sci U S A
Title: Structural basis of cargo recognitions for class V myosins.
Volume: 110
Issue: 28
Pages: 11314-9
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Protein
Q5ND29
Organism: Mus musculus/domesticus
Length: 369  
Fragment?: false
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Protein
Q5FWI3
Organism: Mus musculus/domesticus
Length: 1383  
Fragment?: false
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Protein
Q8BI06
Organism: Mus musculus/domesticus
Length: 1361  
Fragment?: false
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Protein
Q8BH27
Organism: Mus musculus/domesticus
Length: 600  
Fragment?: false
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Publication
14660695 | -
First Author: Cobbe N
Year: 2004
Journal: Mol Biol Evol
Title: The evolution of SMC proteins: phylogenetic analysis and structural implications.
Volume: 21
Issue: 2
Pages: 332-47
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Protein
Q9JJC6
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
Q99LE1
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: false
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Protein
Q8BZ36
Organism: Mus musculus/domesticus
Length: 792  
Fragment?: false
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Protein
Q8K2N8
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: true
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Protein
A0A338P7K9
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: false
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Protein
Q3UI29
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
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Protein
M0QWT5
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: true
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Protein
F7BK35
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: true
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Protein
D3Z376
Organism: Mus musculus/domesticus
Length: 277  
Fragment?: true
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Protein
D6RE39
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
Q8K271
Organism: Mus musculus/domesticus
Length: 976  
Fragment?: true
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Protein
Q80ZE9
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: true
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Protein
G3UX62
Organism: Mus musculus/domesticus
Length: 96  
Fragment?: true
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Protein
Q8C9L7
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Protein
Q9CTN7
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: true
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Protein
F6UPK0
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: true
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Protein
Q9CRX6
Organism: Mus musculus/domesticus
Length: 911  
Fragment?: true
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Protein
A0A087WSM1
Organism: Mus musculus/domesticus
Length: 439  
Fragment?: false
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Protein
D3Z119
Organism: Mus musculus/domesticus
Length: 310  
Fragment?: false
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Protein
Q8C670
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: false
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Protein
A0A140LJ19
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
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Protein
Q60907
Organism: Mus musculus/domesticus
Length: 95  
Fragment?: true
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Protein
F7BG11
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: true
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Protein
Q9D4R7
Organism: Mus musculus/domesticus
Length: 143  
Fragment?: false
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Protein
A0A140LHK7
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: true
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Protein
Q60919
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
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Protein
A0A140LIA3
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
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Protein
Q14AQ2
Organism: Mus musculus/domesticus
Length: 369  
Fragment?: false
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Protein
Q14AX8
Organism: Mus musculus/domesticus
Length: 1361  
Fragment?: false
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Protein
B2RWX4
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: false
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Protein
Q0VGR4
Organism: Mus musculus/domesticus
Length: 600  
Fragment?: false
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Publication
10360576 | -
First Author: Ybe JA
Year: 1999
Journal: Nature
Title: Clathrin self-assembly is mediated by a tandemly repeated superhelix.
Volume: 399
Issue: 6734
Pages: 371-5
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Publication
17702618 | -
First Author: Young A
Year: 2007
Journal: Semin Cell Dev Biol
Title: Structural insights into the clathrin coat.
Volume: 18
Issue: 4
Pages: 448-58
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Publication
10400742 | -
First Author: Bowman MC
Year: 1999
Journal: J Virol
Title: Dissection of individual functions of the Sendai virus phosphoprotein in transcription.
Volume: 73
Issue: 8
Pages: 6474-83
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Publication
18643975 | -
First Author: Petricka JJ
Year: 2008
Journal: Plant J
Title: Vein patterning screens and the defectively organized tributaries mutants in Arabidopsis thaliana.
Volume: 56
Issue: 2
Pages: 251-63
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Publication
9990029 | -
First Author: Reuter W
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus.
Volume: 96
Issue: 4
Pages: 1363-8
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Publication
12682071 | -
First Author: Spitzenberger F
Year: 2003
Journal: J Biol Chem
Title: Islet cell autoantigen of 69 kDa is an arfaptin-related protein associated with the Golgi complex of insulinoma INS-1 cells.
Volume: 278
Issue: 28
Pages: 26166-73
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Publication
11696355 | -
First Author: Cherfils J
Year: 2001
Journal: FEBS Lett
Title: Structural mimicry of DH domains by Arfaptin suggests a model for the recognition of Rac-GDP by its guanine nucleotide exchange factors.
Volume: 507
Issue: 3
Pages: 280-4
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Publication
12730166 | -
First Author: Jensen RB
Year: 2003
Journal: J Bacteriol
Title: Cell-cycle-regulated expression and subcellular localization of the Caulobacter crescentus SMC chromosome structural protein.
Volume: 185
Issue: 10
Pages: 3068-75
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Publication
14980481 | -
First Author: Blanchard L
Year: 2004
Journal: Virology
Title: Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution.
Volume: 319
Issue: 2
Pages: 201-11
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Publication
17459940 | -
First Author: Houben K
Year: 2007
Journal: J Virol
Title: Interaction of the C-terminal domains of sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family.
Volume: 81
Issue: 13
Pages: 6807-16
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Publication
10811823 | -
First Author: Freeman L
Year: 2000
Journal: J Cell Biol
Title: The condensin complex governs chromosome condensation and mitotic transmission of rDNA.
Volume: 149
Issue: 4
Pages: 811-24
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Publication
21399614 | -
First Author: Jakobsen L
Year: 2011
Journal: EMBO J
Title: Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods.
Volume: 30
Issue: 8
Pages: 1520-35
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Publication
19255245 | -
First Author: Komarova Y
Year: 2009
Journal: J Cell Biol
Title: Mammalian end binding proteins control persistent microtubule growth.
Volume: 184
Issue: 5
Pages: 691-706
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Publication
15749712 | -
First Author: Gingerich DJ
Year: 2005
Journal: J Biol Chem
Title: Cullins 3a and 3b assemble with members of the broad complex/tramtrack/bric-a-brac (BTB) protein family to form essential ubiquitin-protein ligases (E3s) in Arabidopsis.
Volume: 280
Issue: 19
Pages: 18810-21
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Publication
15195147 | -
First Author: Guo Y
Year: 2004
Journal: Nat Struct Mol Biol
Title: Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR.
Volume: 11
Issue: 7
Pages: 591-8
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Publication
15509576 | -
First Author: Feinberg H
Year: 2005
Journal: J Biol Chem
Title: Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR.
Volume: 280
Issue: 2
Pages: 1327-35
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Publication
14610287 | -
First Author: Valladeau J
Year: 2003
Journal: Immunol Res
Title: Langerin/CD207 sheds light on formation of birbeck granules and their possible function in Langerhans cells.
Volume: 28
Issue: 2
Pages: 93-107
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Publication
11337487 | -
First Author: Mummidi S
Year: 2001
Journal: J Biol Chem
Title: Extensive repertoire of membrane-bound and soluble dendritic cell-specific ICAM-3-grabbing nonintegrin 1 (DC-SIGN1) and DC-SIGN2 isoforms. Inter-individual variation in expression of DC-SIGN transcripts.
Volume: 276
Issue: 35
Pages: 33196-212
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Publication
12626394 | -
First Author: Stambach NS
Year: 2003
Journal: Glycobiology
Title: Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells.
Volume: 13
Issue: 5
Pages: 401-10
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Publication
21152305 | -
First Author: Massarelli I
Year: 2010
Journal: Int J Mol Sci
Title: Three-dimensional models of the oligomeric human asialoglycoprotein receptor (ASGP-R).
Volume: 11
Issue: 10
Pages: 3867-84
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Publication
16286643 | J:103833
First Author: Park EI
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: The asialoglycoprotein receptor clears glycoconjugates terminating with sialic acid alpha 2,6GalNAc.
Volume: 102
Issue: 47
Pages: 17125-9
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Publication
12499563 | -
First Author: Terawaki S
Year: 2003
Journal: Acta Crystallogr D Biol Crystallogr
Title: Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF).
Volume: 59
Issue: Pt 1
Pages: 177-9
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Publication
22012890 | -
First Author: Yogesha SD
Year: 2011
Journal: Protein Sci
Title: Unfurling of the band 4.1, ezrin, radixin, moesin (FERM) domain of the merlin tumor suppressor.
Volume: 20
Issue: 12
Pages: 2113-20
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Protein Domain
IPR043507 | E_protein_aCoV
Type: Family
Description: This family is specific for E proteins from alphacoronaviruses.E protein is the smallest of the major structural proteins. It is conserved among Coronavirus strains. It is an integral membrane protein involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis []. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virus envelope. The majority of the protein participates in viral assembly and budding [, ]. It can act as a viroporin by oligomerizing after insertion in host membranes to create a hydrophilic pore that allows ion transport [, ]. Additionally, the E protein is thought to prevent M protein aggregation and induce membrane curvature [].SARS-CoV E protein forms a Ca2+ permeable channel in the endoplasmic reticulum Golgi apparatus intermediate compartment (ERGIC)/Golgi membranes. The E protein ion channel activity alters Ca2+ homeostasis within cells boosting the activation of the NLRP3 inflammasome, which leads to the overproduction of IL-1beta. SARS-CoV overstimulates the NF-kappaB inflammatory pathway and interacts with the cellular protein syntenin, triggering p38 MARK activation. These signalling cascades result in exacerbated inflammation and immunopathology [].Cov E proteins have a short hydrophilic N terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficient trafficking of virions. The other would be related to their extramembranedomains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [, , , ]. In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other [].
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Protein Domain
IPR003873 | E_protein_CoV
Type: Family
Description: E protein is the smallest of the major structural proteins. It is conserved among Coronavirus strains. It is an integral membrane protein involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis []. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virus envelope. The majority of the protein participates in viral assembly and budding [, ]. It can act as a viroporin by oligomerizing after insertion in host membranes to create a hydrophilic pore that allows ion transport [, ]. Additionally, the E protein is thought to prevent M protein aggregation and induce membrane curvature [].SARS-CoV E protein forms a Ca2+ permeable channel in the endoplasmic reticulum Golgi apparatus intermediate compartment (ERGIC)/Golgi membranes. The E protein ion channel activity alters Ca2+ homeostasis within cells boosting the activation of the NLRP3 inflammasome, which leads to the overproduction of IL-1beta. SARS-CoV overstimulates the NF-kappaB inflammatory pathway and interacts with the cellular protein syntenin, triggering p38 MARK activation. These signalling cascades result in exacerbated inflammation and immunopathology [].Cov E proteins have a short hydrophilic N terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficient trafficking of virions. The other would be related to their extramembrane domains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [, , , ]. In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other [].
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Protein Domain
IPR043506 | E_protein_bCoV
Type: Family
Description: This family is specific for E proteins from betacoronaviruses.E protein is the smallest of the major structural proteins. It is conserved among Coronavirus strains. It is an integral membrane protein involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis []. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virus envelope. The majority of the protein participates in viral assembly and budding [, ]. It can act as a viroporin by oligomerizing after insertion in host membranes to create a hydrophilic pore that allows ion transport [, ]. Additionally, the E protein is thought to prevent M protein aggregation and induce membrane curvature [].SARS-CoV E protein forms a Ca2+ permeable channel in the endoplasmic reticulum Golgi apparatus intermediate compartment (ERGIC)/Golgi membranes. The E protein ion channel activity alters Ca2+ homeostasis within cells boosting the activation of the NLRP3 inflammasome, which leads to the overproduction of IL-1beta. SARS-CoV overstimulates the NF-kappaB inflammatory pathway and interacts with the cellular protein syntenin, triggering p38 MARK activation. These signalling cascades result in exacerbated inflammation and immunopathology [].Cov E proteins have a short hydrophilic N terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficient trafficking of virions. The other would be related to their extramembrane domains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [, , , ]. In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other [].
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Protein Domain
IPR044377 | E_SARS-CoV-2
Type: Family
Description: This entry represents the Envelope (E) small membrane protein of Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), also known as 2019 novel coronavirus (2019-nCoV) or COVID-19 virus.E protein is the smallest of the major structural proteins. It is conserved among Coronavirus strains. It is an integral membrane protein involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis []. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virus envelope. The majority of the protein participates in viral assembly and budding [, ]. It can act as a viroporin by oligomerizing after insertion in host membranes to create a hydrophilic pore that allows ion transport [, ]. Additionally, the E protein is thought to prevent M protein aggregation and induce membrane curvature [].SARS-CoV E protein forms a Ca2+ permeable channel in the endoplasmic reticulum Golgi apparatus intermediate compartment (ERGIC)/Golgi membranes. The E protein ion channel activity alters Ca2+ homeostasis within cells boosting the activation of the NLRP3 inflammasome, which leads to the overproduction of IL-1beta. SARS-CoV overstimulates the NF-kappaB inflammatory pathway and interacts with the cellular protein syntenin, triggering p38 MARK activation. These signalling cascades result in exacerbated inflammation and immunopathology [].Cov E proteins have a short hydrophilic N terminus, followed by a large hydrophobic transmembrane (TM) domain, and end with a long, hydrophilic C terminus, which comprises the majority of the protein. The hydrophobic region of the TM domain contains at least one predicted amphipathic α-helix that pentamerizes to form an ion-conductive pore in membranes. CoV E proteins have been proposed to have at least two roles. One is related to their TM channel domain. This would be active in the secretory pathway, altering lumenal environments and rearranging secretory organelles and leading to efficient trafficking of virions. The other would be related to their extramembrane domains, particularly the C-terminal domain. This is involved in protein-protein interactions and targeting, among other roles [, , , ]. In the CoV E protein structure a longer α-helix encompasses the TM domain, which is connected to another shorter C-terminal α-helix by a flexible linker domain, forming an L-shape [Li]. The CoV E pentamer is a right handed α-helical bundle where the C-terminal tails coil around each other [].
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