Figure 3
From: An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology

Homology models of the AMY1 receptor ECD (CTR, off-white surface; RAMP1, pink surface) in complex with rAmy (rat amylin, light blue) (a), or CGRPanalog [D31,P34, F35]CGRP27-37 (dark blue) (b), illustrating the predicted mode of peptide binding at the AMY1 receptor. The surfaces of key residues mutated in the current study are highlighted according to the magnitude of effect of mutation on peptide function (red, >50-fold decreased potency; orange, 10–50-fold decreased potency; yellow, <10-fold decreased potency; and blue, not significantly different). (c and d) illustrate how the peptides interact with the peptide-binding groove. Receptor residues are in off-white x-stick, RAMP1 residue W84 is in orange and the peptides are blue. Peptide amino acid numbers are displayed as superscript and receptor numbers in normal type. Hydrogen bonds are illustrated as coloured spheres. (c) rAmy (rat amylin). (d) CGRP analogue.