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. 2022 Nov 16;13:7013. doi: 10.1038/s41467-022-34629-3

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a, b VPAC1R-VIP (green), VPAC1R-PACAP27 (blue) and PAC1R-PACAP27 (pink) atomic coordinate frames derived from the cryoSPARC 3DVA extreme frames (frame 0 and 19) from each component (component 0 to 2) were overlayed and different frames were coloured in a colour gradient according to their peptide-receptor pair (Comp 0, frame 0 lowest saturation, Comp 2, frame 19 highest saturation). c–f Snapshots of the MD equilibrium simulation from the experimental structures of VPAC1R-PACAP27, PAC1R-PACAP27 and VPAC1R-VIP, as well as the PAC1R-VIP homology model (as indicated by asterisk *). Simulations were run without the ECD-ECL1 disulfide bond present. Snapshots were extracted from the simulations as PDBs (extracting every 100th frame), opened in Chimera and coloured by Cα RMSD in Å, in a colour scale from 0 Å = blue to 16 Å = red. The receptor and peptide backbones are displayed in ribbon format and shown as front view of the receptor TMs and peptide and top view. ECD residues of the PAC1R and VPAC1R receptor are not displayed for clarity. For the PAC1R-VIP homology model, the MD simulations did not consider the full-length Gs protein (only the Gα H5 was retained).