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. 2022 Feb 25;13:1057. doi: 10.1038/s41467-022-28683-0

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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. 4 — a Structural comparison of peptide 20–GIPR–G_s, peptide 20–GLP-1R–G_s and peptide 20–GCGR–G_s. Receptor ECD and G protein are omitted for clarity. b–d Interactions between peptide 20 and the TMDs of GIPR (forest green), GLP-1R (blue), and GCGR (hot pink). Residues involved in interactions are shown as sticks. e–g Surface representations of the receptor for each of the peptide-receptor complex, with the peptides shown as ribbon and sticks. The receptor is shown in surface representation and colored from dodger blue for the most hydrophilic region, to white, to orange red for the most hydrophobic region. h The peptide recognition modes are described by fingerprint strings encoding different interaction types of the surrounding residues in each receptor. Color codes are listed on the top panel. Residues that show no interaction with receptors are displayed as white circles.