Author(s): Burbach JP, Meijer OC, Burbach JP, Meijer OC
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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.
This article was published in Eur J Pharmacol
and referenced in Cancer Surgery