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. 2021 Apr 28;594(7864):594–598. doi: 10.1038/s41586-021-03507-1

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© The Author(s) 2021

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. 3 — a, The G_i1 binding pocket in GABA_B, which is mainly formed by three intracellular loops of GB2. GB2, green; Gα_i1, yellow. b, c, Detailed interactions of the ICL2 and TM3 of GB2 with Gα_i (b), and of ICL1 and ICL3 with Gα_i (c). d, Baclofen-induced IP1 accumulation using Gα_qi9. Bars represent differences in calculated E_max and basal activity or potency (pEC₅₀) for each mutant as a percentage of the maximum in wild type. Data are mean ± s.e.m. from at least three independent experiments, performed in technical triplicate and analysed using one-way analysis of variance with Dunnett’s multiple comparison test to determine significance (compared with wild type). ND, not determined; NS, not significant. e, The C^G.H5.23 and G^G.H5.24 residues in the C-terminal α5 helix of Gα_i are involved in the selective coupling between GABA_B and G_i protein. The α5-helix structures of G_s (PDB 5VAI), G_q (PDB 6WHA) and the GABA_B-bound G_i were aligned. f, g, Effect of C^G.H5.23 (f) and G^G.H5.24 (g) mutations in Gα_i on GABA_B–G_i coupling using NanoBiT G-protein dissociation assay. Data are mean ± s.e.m. from at least three independent experiments.

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