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. 2022 Sep 5;13:5232. doi: 10.1038/s41467-022-32822-y

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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 Overview of the Gαi (pink) interacting with FPR1 (green, left) and FPR2 (blue, middle, PDB ID: 6OMM). The structures are front view from the intracellular side, showing in cartoon overlap with surface in 50% transparency. The crystal structure of FPR2 (right) is colored in olive and showed in cartoon and surface. b Slab view showing the interactions between FPR1 and Gαi protein (left). The region TM2, TM3, TM6, and ICL3 of FPR1 form direct contact with α5 helix of Gαi protein (middle). C126 in TM3, Y64 in TM2 forms hydrogen bond to N347, N351 in α5 helix of Gαi protein, respectively. ICL2 of FPR1 has polar interactions with αN helix and β1-β2 loop of Gαi protein (right). c Slab view showing the interactions between FPR2 and α5 helix of Gαi protein (left), as well as interactions of ICL2 of FPR2 with αN helix and β1-β2 loop of Gαi protein (right).