Fig. 3: Differential interactions of P37Cagri, Y37rAmy and P32sCT with AMYRs.
From: Structural and dynamic features of cagrilintide binding to calcitonin and amylin receptors
a–e model comparison of the interactions of C-terminal residues of Cagri, rAmy and sCT with receptor ECDs: (a) P37Cagri-AMY1R vs Y37rAmy-AMY1R, (b) P37Cagri-AMY1R vs P32sCT-AMY1R, (c) P37Cagri-AMY2R vs Y37rAmy-AMY2R, and (d) P37Cagri-AMY2R vs P32sCT-AMY2R, (e) P37Cagri-AMY3R vs Y37rAmy-AMY3R. Structures were aligned on the ECD (residues 41-138) of the CTR protomer with protein backbone displayed in ribbon format. H-bonds are shown as dashed lines. The rigid-body translocations of RAMP ECD in the presence of Cagri relative to the rAmy are highlighted by the red arrows. f Map to model representation of the ECD interface of RAMP3 and CTR in complex with Cagri. The displayed map was contoured to 0.234.
