Molecular structure and mechanisms of action of mammalian angiotensin II receptors

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Abstract
Two pharmacologically distinct types of mammalian angiotensin II receptors have been defined and designated ATI and AT2. Cloning of these receptor complementary DNAs has elucidated their primary structure and indicates that they both belong to the G protein-coupled receptor family. All the known physiological actions of angiotensin II are mediated by the AT1 receptors. In vitro mutagenesis studies have shown that the angiotensin II binding site of the AT1 receptor involves residues of the extracellular loops, whereas nonpeptidic antagonists bind to polar residues of the transmembrane domains. Similar studies have identilied the residues required for G protein coupling to lie in the intracellular loops and those involved in internalization to be in the carboxyl terminal segment. The AT2 receptor signaling pathway appears to modulate tyrosine phosphatase activity and to regulate the opening of ion channels. The physiological roles of this receptor are poorly understood but may include regulation of natriuresis and inhibition of endothelial cell proliferation.

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