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. 2022 Sep 20;13:5513. doi: 10.1038/s41467-022-33173-4

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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. 5 — a An overall comparison of αH5 engagements of Gα_q, Gα_s, Gα_i, Gα₁₂ and Gα₁₃ to receptor. Receptor was drawn in hydrophobic surface potential. b A comparison of the very end of αH5 of G-proteins in engagements of GPR110. Left panel, superimposition of αH5 of Gα_q, Gα_s, Gα_i, Gα₁₂ and Gα₁₃ in GPR110 engagements; right panel, an alignment of the last 8 residues of αH5 of Gα_q, Gα_s, Gα_i, Gα₁₂ and Gα₁₃. Brown color marks hydrophobic residues, cyan color marks polar residues, blue color marks negative charged residues and red color marks positive charged residues. c A comparison of the G_q and G_s engagements with GPR110. d A comparison of the G_i, G₁₃ and G₁₂ engagements with GPR110. e A connective interaction map of the αH5/receptor interaction of the Gα_q, Gα_s, Gα_i, Gα_12, Gα₁₃/receptor complexes. The thick blue line marks hydrogen bond between side chains, the light and thin blue line marks hydrogen bond between side chain and backbone, the brown line marks hydrophobic interaction.