Characteristics of Anti-CXC-R3/CD183 (Chemokine receptorC-X-C chemokine receptor type 3)

CXC chemokine receptors are basic film proteins that accurately bind and acknowledge to cytokines of the CXC chemokine family. They represent one subfamily of chemokine receptors, a ample ancestors of G protein-linked receptors that are accepted as seven transmembrane (7-TM) proteins, back they amount the corpuscle film seven times. There are currently seven accepted CXC chemokine receptors in mammals, alleged CXCR1 through CXCR7.
CXCR3 is bidding predominantly on T lymphocytes, and aswell on added lymphocytes (some B beef and NK cells) and is awful induced afterward corpuscle activation. There are two isoforms, CXCR3-A and CXCR3-B. It has three awful accompanying ligands in mammals, CXCL9, CXCL10 and CXCL11.
Chemokine receptors are cytokine receptors begin on the apparent of assertive beef that collaborate with a blazon of cytokine alleged a chemokine. There accept been 19 audible chemokine receptors declared in mammals. Each has a 7-transmembrane (7TM) anatomy and couples to G-protein for arresting transduction aural a cell, authoritative them associates of a ample protein ancestors of G protein-coupled receptors. Afterward alternation with their specific chemokine ligands, chemokine receptors activate a alteration in intracellular calcium (Ca2+) ions (calcium signaling). This causes corpuscle responses, including the access of a action accepted as chemotaxis that traffics the corpuscle to a adapted area aural the organism. Chemokine receptors are disconnected into altered families, CXC chemokine receptors, CC chemokine receptors, CX3C chemokine receptors and XC chemokine receptors that accord to the 4 audible subfamilies of chemokines they bind.
Characteristics
Chemokine receptors are G protein-coupled receptors absolute 7 transmembrane domains that are begin predominantly on the apparent of leukocytes. Approximately 19 altered chemokine receptors accept been characterized to date, which allotment abounding accepted structural features; they are composed of about 350 amino acids that are disconnected into a abbreviate and acerb N-terminal end, seven circling transmembrane domains with three intracellular and three extracellular hydrophilic loops, and an intracellular C-terminus absolute serine and threonine residues that act as phosphorylation sites during receptor regulation. The aboriginal two extracellular loops of chemokine receptors are affiliated calm by disulfide bonding amid two conserved cysteine residues. The N-terminal end of a chemokine receptor binds to chemokine(s) and is important for ligand specificity. G-proteins brace to the C-terminal end, which is important for receptor signaling afterward ligand binding. Although chemokine receptors allotment top amino acerbic character in their primary sequences, they about bind a bound amount of ligands.
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