title: The structure of neuropeptide receptors.
abstract: Recently, the primary structures of 17 different receptors for neuropeptides and small peptide hormones have been elucidated by molecular cloning. All but one belong to the superfamily of G-protein coupled receptors which share a topography consisting of seven transmembrane domains. Comparison of primary structures shows that two classes of peptide receptors exist. One referred to as the 'neurokinin-type receptors', possesses many of the typical, conserved amino acid sequence motifs of the aminergic transmitter receptors (e.g. beta-adrenoceptor). The other, referred to the 'secretin-type receptors', displays unrelated and distinctly different sequence motifs which are conserved between the three presently known members of this class. These are the secretin, calcitonin and parathyroid hormone/parathyroid hormone-like polypeptide receptors. One may speculate that many other peptides with a core of biological activity in the N-terminal or middle region may have receptors of the secretin-type.
authors.affiliation: Rudolf Magnus Institute, Department of Pharmacology, Utrecht University, Netherlands.
authors.forename: J P
authors.initials: JP
authors.lastname: Burbach
authors.forename: O C
authors.initials: OC
authors.lastname: Meijer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003001:Cloning, Molecular; D019204:GTP-Binding Proteins / Q000502:physiology; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000378:metabolism* / Q000502:physiology; D051381:Rats; D017981:Receptors, Neurotransmitter / Q000737:chemistry* / Q000648:ultrastructure*
chemical_list: D009479:Neuropeptides; D017981:Receptors, Neurotransmitter; D019204:GTP-Binding Proteins