THE STRUCTURE OF NEUROPEPTIDE RECEPTORS

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 as 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.