This α-helical dimerisation domain is found in alkyl/aryl-sulfatases such as the Saccharomyces cerevisiae BDS1 (). BDS1 enables the use of SDS and 4-nitrocatechol as sulfur source [].
Spermidine export protein MdtJ catalyzes the excretion of spermidine. It can also confer resistance to deoxycholate and SDS [, ]. It is induced by spermidine.
Spermidine export protein MdtI catalyzes the excretion of spermidine. It can also confer resistance to deoxycholate and SDS [, ]. It is integral to membrane [].
This entry represents a group of arylsulfatases, including Bds1 from budding yeasts, SdsA1 from Pseudomonas aeruginosa and YjcS from E. coli. SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source [, ]. SdsA1 also contributes to the in vivo virulence of P. aeruginosa by playing a central role in the degradation of mucin []. YjcS is also able to cleave SDS []. Bds1, also known as bacterially-derived sulfatase, is required for use of alkyl- and aryl-sulfates as sulfur sources [].
This superfamily includes the F1 beta subunit of ATP synthase.F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.The NMR solution structure of the protein in SDS micelles was found to contain two helices, an N-terminal amphipathic α-helix and a C-terminal α-helix separated by a large unstructured internal domain. The N-terminal α-helix is the Tom20 receptor binding site whereas the C-terminal α-helix is located upstream of the mitochondrial processing peptidase cleavage site [].
F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. This entry represents the beta subunit of the F1 component.The NMR solution structure of the protein in SDS micelles was found to contain two helices, an N-terminal amphipathic α-helix and a C-terminal α-helix separated by a large unstructured internal domain. The N-terminal α-helix is the Tom20 receptor binding site whereas the C-terminal α-helix is located upstream of the mitochondrial processing peptidase cleavage site [].
Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating physical properties of the membrane, such as mechanical stability and de-formability, by stabilising spectrin-actin interactions [, , ]. It is required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase [].The protein has been shown to associate with the nuclear mitotic apparatus, the contractile apparatus and tight junctions. Defects in this protein can cause elliptocytosis type 1 and hereditary pyropoikilocytosis.Note: Band 4.1 and Band 7 () proteins refer to human erythrocyte membrane proteins separated by SDS polyacrylamide gels and stained with coomassie blue [].
Dpl is a homologue related to the prion protein (PrP). Dpl is toxic to neurons and is expressed in the brains of mice that do not express PrP. In DHPC and SDS micelles, Dpl shoes about 40% α-helical structure however in aqueous solution it consists of a random coil. The alpha helical segment can adopt a transmembrane localisation also in a membrane. The unprocessed Dpl protein is thought to posses a possible channel formation mechanism which may be related to toxicity through direct interaction with cell membranes and damage to the cell membrane.
The band-7 protein family comprises a diverse set of membrane-bound proteins characterised by the presence of a conserved domain, the band-7 domain, also known as SPFH or PHB domain []. The exact function of the band-7 domain is not known, but examples from animal and bacterial stomatin-type proteins demonstrate binding to lipids and the ability to assemble into membrane-bound oligomers that form putative scaffolds []. A variety of proteins belong to this family. These include the prohibitins, cytoplasmic anti-proliferative proteins and stomatin, an erythrocyte membrane protein. Bacterial HflC protein also belongs to this family.Note: Band 4.1 and Band 7 proteins refer to human erythrocyte membrane proteins separated by SDS polyacrylamide gels and stained with coomassie blue [].
This entry represents band 4.1-like protein 2 []. It shares protein sequence similarity with Band 4.1 protein. Its function is not clear.Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating physical properties of the membrane, such as mechanical stability and de-formability, by stabilising spectrin-actin interactions [, , ]. It is required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase [].The protein has been shown to associate with the nuclear mitotic apparatus, the contractile apparatus and tight junctions. Defects in this protein can cause elliptocytosis type 1 and hereditary pyropoikilocytosis.Note: Band 4.1 and Band 7 () proteins refer to human erythrocyte membrane proteins separated by SDS polyacrylamide gels and stained with coomassie blue [].
The band-7 protein family comprises a diverse set of membrane-bound proteins characterised by the presence of a conserved domain, the band-7 domain, also known as SPFH or PHB domain []. The exact function of the band-7 domain is not known, but examples from animal and bacterial stomatin-type proteins demonstrate binding to lipids and the ability to assemble into membrane-bound oligomers that form putative scaffolds []. A variety of proteins belong to this family. These include the prohibitins, cytoplasmic anti-proliferative proteins and stomatin, an erythrocyte membrane protein. Bacterial HflC protein also belongs to this family.Note: Band 4.1 and Band 7 proteins refer to human erythrocyte membrane proteins separated by SDS polyacrylamide gels and stained with coomassie blue [].
The calcitonin (CT) gene is alternatively expressed in a tissue-specific manner, producing either the calcium regulatory hormone CT in the thyroid, or the neuropeptide calcitonin gene related peptide (CGRP) in the brain []. In medullary carcinoma of the thyroid, both peptides are produced []. The calcitonin regulatory hormone is a peptide of 32 residues that causes a rapid but short-lived drop in calcium and phosphate levels in the blood by promoting the incorporation of these ions in the bones []. The structure of Oncorhynchus keta (Chum salmon) calcitonin has been studied by 2D NMR in SDS micelles []. The main conformational feature of the hormone is an α-helix from residues 6-22, which includes an amphipathic segment. Two cysteine residues (at positions 1 and 7) form an N-terminal loop, and a C-terminal decapeptide forms a loop that folds back towards the helix [].
The anti-apoptotic protein p35 from baculovirus is thought to prevent the suicidal response ofinfected insect cells by inhibiting caspases. Ectopic expression of p35 in a number of transgenic animals or cell lines is also anti-apoptotic, giving rise to the hypothesis that the protein is a general inhibitor of caspases. This protein belongs to MEROPS proteinase inhibitor family I50, clan IQ. Purified recombinant p35 inhibits human caspase-1, -3, -6, -7, -8, and -10 but does not significantly inhibit unrelated serine or cysteine proteases, implying that p35 is a potent caspase-specific inhibitor. The interaction of p35 with caspase-3, as a model of the inhibitory mechanism,revealed classic slow-binding inhibition, with both active-sites of the caspase-3 dimer acting equally and independently. Inhibition resulted from complex formation between the enzyme and inhibitor, which could be visualised under non-denaturing conditions, but was dissociated by SDS to give p35 cleaved at Asp87, the P1 residue of the inhibitor. Complex formation requires the substrate-binding cleft to be unoccupied [].Infecting the insect cell line IPLB-Ld652Y with the baculovirus Autographa californica nuclear polyhedrosis virus (AcMNPV) results in global translation arrest, which correlates with the presence of the AcMNPV apoptotic suppressor, p35. However, the anti-apoptotic function of p35 in translation arrest is not solely due to caspase inactivation, but its activity enhances signalling to a separate translation arrest pathway, possibly by stimulating the late stages of the baculovirus infection cycle []. The baculovirus p35 structure forms a sandwich composed of 14 strands in 2 sheets with a greek-key topology.
The anti-apoptotic protein p35 from baculovirus is thought to prevent the suicidal response ofinfected insect cells by inhibiting caspases. Ectopic expression of p35 in a number of transgenic animals or cell lines is also anti-apoptotic, giving rise to the hypothesis that the protein is a general inhibitor of caspases. This protein belongs to MEROPS proteinase inhibitor family I50, clan IQ. Purified recombinant p35 inhibits human caspase-1, -3, -6, -7, -8, and -10 but does not significantly inhibit unrelated serine or cysteine proteases, implying that p35 is a potent caspase-specific inhibitor. The interaction of p35 with caspase-3, as a model of the inhibitory mechanism,revealed classic slow-binding inhibition, with both active-sites of the caspase-3 dimer acting equally and independently. Inhibition resulted from complex formation between the enzyme and inhibitor, which could be visualised under non-denaturing conditions, but was dissociated by SDS to give p35 cleaved at Asp87, the P1 residue of the inhibitor. Complex formation requires the substrate-binding cleft to be unoccupied [].Infecting the insect cell line IPLB-Ld652Y with the baculovirus Autographa californica nuclear polyhedrosis virus (AcMNPV) results in global translation arrest, which correlates with the presence of the AcMNPV apoptotic suppressor, p35. However, the anti-apoptotic function of p35 in translation arrest is not solely due to caspase inactivation, but its activity enhances signalling to a separate translation arrest pathway, possibly by stimulating the late stages of the baculovirus infection cycle [].
The calcitonin (CT) gene is alternatively expressed in a tissue-specific manner, producing either the calcium regulatory hormone CT in the thyroid, or the neuropeptide calcitonin gene related peptide (CGRP) in the brain []. In medullary carcinoma of the thyroid, both peptides are produced [].The calcitonin regulatory hormone is a peptide of 32 residues that causes a rapid but short-lived drop in calcium and phosphate levels in the blood by promoting the incorporation of these ions in the bones []. The structure of Oncorhynchus sp. (Salmon) calcitonin has been studied by 2D NMR in SDS micelles []. The main conformational feature of the hormone is an α-helix from residues 6-22, which includes an amphipathic segment. Two cysteine residues (at positions 1 and 7) form an N-terminal loop, and a C-terminal decapeptide forms a loop that folds back towards the helix [].CGRP is a 37-residue peptide produced by alternative splicing of the CT gene. CGRP induces vasodilation in various vessels, including those of the coronary, cerebral and systemic vasculature. A neurotransmitter or neuro-modulator role is suggested by its abundance in the CNS []. The structure of human CGRP has been determined by 1H NMR []. The main conformational feature of the hormone is an N-terminal disulphide-bonded loop (residues 2-7), leading into a well-defined α-helix between residues 8 and 18; thereafter, the structure is predominantly disordered, althoughthere are indications of a preference for a turn-type conformation between residues 19 and 21 [].This entry represents the full-length propeptide (procalcitonin gene-related peptide or proCGRP) before cleavage into the calcitonin peptide.
