Chemoattractant receptors

Leukocyte chemoattractant receptor primary structures have been deduced from cloned cDNAs for N-formyl peptides, C5a, platelet-activating factor and eight of the chemokines. All of the receptors are seven-transmembrane domain rhodopsin-like G pro-tein-coupled receptors. Their sequences are all approximately 350 amino acids in length and they share greater than 20% amino acid identity with each other. A general structural model of these receptors has been developed from a statistical analysis of sequences found in the hydrophobic domains and the known structures of rhodopsin and bacteriorhodop-sin. The primary structural features include 1) an extracellular amino-terminus, 2) an intracellular car-boxy-terminus, 3) seven a-helical transmembrane domains that are oriented perpendicularly to the plasma membrane, with kinks occurring in transmembrane domains II, IV, V, VI and VII by intra-helical prolines, and 4) three intracellular and three extracellular connecting loops comprised of hydro-philic amino acids. The amino-terminal segments of the receptors are usually acidic and contain potential sites for asparagine-linked glycosylation. The car-boxy-termini are rich in serine and threonine residues, which may serve as phosphorylation sites for receptor desensitization, as occurs for rhodopsin and ß2-adrenergic receptors.

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