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 language | English |
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Pages (from-to) | 451-455 |
Number of pages | 5 |
Journal | Biochemical Society Transactions |
Volume | 30 |
DOIs | |
Publication status | Published - 1 Aug 2001 |
Keywords
- calcitonin-receptor-like receptor (CRLR)
- structure-activity relationships
- receptor-activity-modifying protein I (RAMPI)
- adrenomedullin
- CGRP