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. 2022 Nov 17;13:7033. doi: 10.1038/s41467-022-34696-6

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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 Interactions between the C-terminus of Gα α5 helix and GPR119. The π-π interaction between Gα_s and GPR119 is shown. b F111^ICL2 of GPR119 docks into a hydrophobic pocket on the Gα_s surface. c The salt bridge between ICL1 in GPR119 and Gα_s or Gβ1. d Interactions between TM5 of GPR119 and Gα_s. e cAMP accumulation of GPR119 induced by agonist AR231453. WT were repeated 18 times. Other mutants were all repeated 3 times. *P < 0.01; ***P < 0.0001 by one-way ANOVA followed by Dunnett’s post-test, compared with the response of the WT. A detailed statistical evaluation is provided in Supplementary table 2. Source data are available as a Source Data file.