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. 2023 Sep 23;14:5938. doi: 10.1038/s41467-023-41646-3

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© The Author(s) 2023

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 Key residue clashes and conformational changes induced by binding of compound 1 (Cpd 1) to GPR61. The structure of active GPR61 (light grey) is overlaid with the compound 1 (magenta)-bound structure of inactive GPR61 (blue), with key residues highlighted in stick representation. Clashes with the compound are indicated by red stars, while clashes with Gαs induced by compound binding are indicated by yellow stars. b Compound 1 defines an unusual allosteric site and mechanism. The structure of compound 1-bound GPR61_IA is shown in ribbon representation, with published exemplars^45,62–68 representing the known allosteric sites of class A GPCRs superimposed, colored as indicated. c Compound 1-bound GPR61_IA and vercirnon-bound CCR9⁴⁵ structures, colored as indicated, are superimposed. Vercirnon occupies the known allosteric site that lies nearest to that of compound 1. The different conformations of TM6 induced by these two inverse agonists are highlighted.