Structure-activity relationships of neuropeptide Y analogues with respect to Y1 and Y2 receptors.
Secondary structure investigations, affinities, and activities of neuropeptide Y analogues with respect to the Y1 and the Y2 receptor are reviewed. The results are discussed with respect to the different prerequisites for affinities to both receptor subtypes. The results from a systematic scanning of the hormone using L-alanine and from a large variety of discontinuous and cyclic analogs suggest that two different conformations of neuropeptide Y are adopted at the Y1 and Y2 receptors. Whereas a C-terminal turn structure is suggested for Y1 receptor affinity, an alpha-helical conformation of the C-terminus is afforded for good binding to the Y2 receptor.
Beck-Sickinger
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AG
Institute of Organic Chemistry, University of Tübingen, Germany.
Jung
G
G
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009478:Neuropeptide Y / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D017433:Protein Structure, Secondary; D017476:Receptors, Neuropeptide Y / Q000187:drug effects / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D013045:Species Specificity; D013329:Structure-Activity Relationship
D009478:Neuropeptide Y; D017476:Receptors, Neuropeptide Y