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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. 6 — a Comparison of G protein coupling among GIPR, GLP-1R and GCGR^{4, 25, 27}. The Gα_s α5-helix of the Gα_s Ras-like domain inserts into an intracellular crevice of receptor’s TMD. The receptors and G proteins are colored as the labels. b Comparison of ICL2 conformation in the peptide 20-bound GIPR, GCGR and GLP-1R. c Comparison of F257^3.60b conformation in the GLP-1R bound by GLP-1, tirzepatide and peptide 20. d Comparison of E262^ICL2 conformation in the GLP-1R bound by GLP-1, tirzepatide and peptide 20. e Comparison of E253^ICL2 conformation in the GIPR bound by tirzepatide and peptide 20. Residues involved in interactions are shown as sticks. Polar interactions are shown as black dashed lines.