Molecular characterization of the ligand-receptor interaction of neuropeptide Y.
Neuropeptide Y (NPY) consists of 36 amino acids and is one of the most abundant peptides in the peripheral and central nervous system. Several subtypes of NPY receptors have been described (Y1- y6) using segments and analogues of NPY. The Y1-, Y2- and the Y5-receptor, which have been cloned, belong to the G-protein coupled hormone receptor family and will be specially addressed, because they are the endogenous binding sites of neuropeptide Y in human. In contrast, Y4-receptors recognize endogenous PP, Y3 receptors are discussed controversially and the y6-receptor is truncated in human. In this review, we summarize the data of neuropeptide Y with respect to ligand binding, selectivity, receptor structures and ligand-receptor complexes by using ligand analogues, site directed mutagenesis and photoaffinity labeling.
Ingenhoven
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Swiss Federal Institute of Technology Zürich, Department of Pharmacy, Winterthurer Str. 190, Zürich, CH 8057, Zürich.
Beck-Sickinger
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AG
D000595:Amino Acid Sequence; D000818:Animals; D001067:Appetite Depressants / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D009478:Neuropeptide Y / Q000737:chemistry / Q000494:pharmacology*; D017476:Receptors, Neuropeptide Y / Q000737:chemistry / Q000187:drug effects*
D001067:Appetite Depressants; D008024:Ligands; D009478:Neuropeptide Y; D017476:Receptors, Neuropeptide Y