Interaction of calcitonin-gene-related peptide with its receptors

Alex C. Conner, Debbie L. Hay, S.G. Howitt, K. Kilk, U. Langel, Mark Wheatley, David M. Smith, David R. Poyner

Research output: Contribution to journalArticlepeer-review

Abstract

The receptor for calcitonin-gene-related peptide (CGRP) is a heterodimer formed by calcitonin-receptor-like receptor (CRLR), a type II (family B) G-protein-coupled receptor, and receptor-activity-modifying protein 1 (RAMP1), a single-membrane-pass protein. It is likely that the first seven or so amino acids of CGRP (which form a disulphide-bonded loop) interact with the transmembrane domain of CRLR to cause receptor activation. The rest of the CGRP molecule falls into three domains. Residues 28-37 and 8-18 are normally required for high-affinity binding, while residues 19-27 form a hinge region. The 28-37 region is almost certainly in direct contact with the receptor; 8-18 may make additional receptor contacts or may stabilize an appropriate conformation of 28-37. It is likely that these regions of CGRP interact both with CRLR and with the extracellular domain of RAMP1.
Original languageEnglish
Pages (from-to)451-455
Number of pages5
JournalBiochemical Society Transactions
Volume30
Issue number4
DOIs
Publication statusPublished - 28 Aug 2002

Bibliographical note

Colloquium on Lessons from the Type II Family of G-Protein-Coupled Receptores - Their Ligands, Receptor Structure and Function, Edinburgh (UK), 8-10 April 2002

Keywords

  • adrenomedullin
  • calcitonin-receptor-like receptor (CRLR)
  • CGRP
  • receptor-activity-modifying protein 1 (RAMPI)
  • structure-activity relationships

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