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Search results 1 to 4 out of 4 for Ccr2

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role []. They have a wide range of effects in many different cell types beyond the immune system, including, for example, various cells of the central nervous system [], and endothelial cells, where they may act as either angiogenic or angiostatic factors [].The chemokine family is divided into four classes based on the number and spacing of their conserved cysteines: 2 Cys residues may be adjacent (the CC family); separated by an intervening residue (the CXC family); have only one of the first two Cys residues (C chemokines); or contain both cysteines, separated by three intervening residues (CX3C chemokines).Chemokines exert their effects by binding to rhodopsin-like G protein-coupled receptors on the surface of cells. Following interaction with their specific chemokine ligands, chemokine receptors trigger a flux in intracellular calcium ions, which cause a cellular response, including the onset of chemotaxis. There are over fifty distinct chemokines and least 18 human chemokine receptors []. Although the receptors bind only a single class of chemokines, they often bind several members of the same class with high affinity. Chemokine receptors are preferentially expressed on important functional subsets of dendritic cells, monocytes and lymphocytes, including Langerhans cells and T helper cells [, ]. Chemokines and their receptors can also be subclassified into homeostatic leukocyte homing molecules (CXCR4, CXCR5, CCR7, CCR9) versus inflammatory/inducible molecules (CXCR1, CXCR2, CXCR3, CCR1-6, CX3CR1).CC chemokine receptors are a subfamily of the chemokine receptors that specifically bind and respond to cytokines of the CC chemokine family. There are currently ten members of the CC chemokine receptor subfamily, named CCR1 to 10. The receptors receptors are found in monocytes, lymphocytes, basophils and eosinophils.This entry represents CC chemokine receptor 2 (CCR2), it is a receptor for the monocyte chemoattractant protein-1 (CCL2), a chemokine which specifically mediates monocyte chemotaxisis involved in monocyte infiltration in inflammatory diseases such as rheumatoid arthritis []as well as in the inflammatory response against tumors []. It has also been shown that CCR2 deficient mice develop an accelerated Alzheimer's-like pathology in comparison to wild type mice [, , ]. CCR2 has also been shown to function in blood vessel remodeling []. Following interaction with specific CC chemokine ligands, CCR2 triggers a flux in intracellular calcium ions [, ]and inhibition of adenylyl cyclase []. This causes cell responses, including the recruitment of mononuclear phagocytes into the CNS, leading to chemotaxis [].
Protein Domain
Type: Family
Description: This family includes plant serine/threonine receptor-like kinases related to CRINKLY4 (CR4), a protein involved in developmental processes in plant and endosperm that was first isolated in maize [, ]. Mutations in this protein affects the cell wall thickness and structure, cuticle formation, and vesicle trafficking, and tumor like outgrowths, with similar effects seen in rice [, , ]. Arabidopsis thaliana contains an orthologue of CR4, ACR4, and four CRINKLY4-related proteins (CRR or CCR) AtCRR1, AtCRR2, AtCRR3 and AtCRR4 (also known as CRINKLY 4-related kinase 1, AtCRK1) []. Phylogenetic analysis showed that the CR4 family of receptor kinases can be divided in three clades, one including CR4, CCR1 and CCR2, a second including CCR3 and CCR4 family members, and a third and more distant clade including members from algae and Selaginella moellendorffii sequences with transmembrane and/or kinase domains []. Kinase assays showed that ACR4 is an active serine/threonine kinase, while CCR1 and CCR2 are nearly inactive in autophosphorylation assays []. CR4 family are characterised by the presence of seven 'crinkly' repeats in the extracellular part which is required both for signalling and normal protein internalisation, including a conserved C(X~10)CWG sequence motif. The Cys residues in the extracellular 'crinkly' repeat domain are likely to form stabilizing disulfide bridges []. Another feature of the CR4 family is that the extracellular domain shows homology to the three Cys-rich repeats of the TUMOR NECROSIS FACTOR RECEPTOR (TNFR) extracellular domain [].This family represents the CRINKLE4-related proteins CCR3 and CCR4.
Protein Domain
Type: Family
Description: This is a family of nucleoporins conserved from yeast to human.Nup85 Nucleoporin is an essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP98/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol-3-kinase-Rac-lammellipodium protrusion cascade [, , ]. The Nup84 complex is composed of one copy each of Nup84, Nup85, Nup120, Nup133, Nup145C, Sec13, and Seh1. The structure of a complex of Nup85 and Seh1 was solved []. The N terminus of Nup85 is inserted and forms a three-stranded blade that completes the Seh1 6-bladed β-propeller in trans. Following its N-terminal insertion blade, Nup85 forms a compact cuboid structure composed of 20 helices, with two distinct modules, referred to as crown and trunk [].
Protein Domain
Type: Family
Description: Human herpesvirus 6A (HHV-6A) and HHV-6B are classified as roseoloviruses and are highly prevalent in the human population. Roseolovirus reactivation in an immunocompromised host can cause severe pathologies []. HHV6 A/B encode two putative chemokine receptors and a chemokine-like protein. The HHV6 U83 gene encodes a CC chemokine, which functions as a highly selective and efficacious agonist for the human CCR2 receptor, both in respect of signal transduction and the ability to induce chemotaxis. Homologues of the U83 gene products are found in Human cytomegalovirus encoded chemokines vCXC1 and vCXC2.HHV-6 U83, also known as vCCL4, contains a region with the CC/CX3C chemokine motif and a glycosaminoglycan (GAG)-binding epitope, BBXB (B being a basic residue), found right before the third Cys residue, which very likely forms a disulfide bridge back to the first Cys of the protein []. This gene is the only HHV-6A/B divergent gene that is specific for these viruses. The U83 chemokine gene is distinct between HHV-6A and HHV-6B strains, encoding up to 13 amino acid differences. The HHV-6A (U83A) and HHV-6B (U83B) chemokines have distinct specificities which determine chemoattraction or diversion of different leukocyte subsets for infection or immune evasion, thus an early component of cellular tropism as well as mediator of innate immunity. U83 also has a varied gene structure, with N-terminal length variation determining production of the encoded mature secreted chemokine, coupled with control by cell-directed splicing which truncates the chemokine gene early in replication to encode an antagonist. The 'long' active form of U83A has a unique broad specificity for receptors CCR1, CCR4, CCR5, CCR6 and CCR8 present on plasmacytoid and myeloid dendritic and monocyte/macrophage antigen presenting cells, as well as both TH1 and TH2 skin homing lymphocytes and NK cells; it is also amongst the highest affinity ligands for CCR5 and inhibits HIV-1 binding at this coreceptor. U83A can both block and divert human chemokine action while occupying the human chemokine receptors [].