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. 2024 Dec 5;15:10601. doi: 10.1038/s41467-024-54681-5

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/.

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Fig. 4 — a Detailed interactions of the transmembrane interface in the apo GPR156. The 7TM homodimer interface is formed at two regions (I and II), namely the extracellular and intracellular side. b Detailed interactions on the surface of the region I. The network of electrostatic interactions is shown in Ia, and the affiliated hydrophobic interaction is shown in Ib. c Detailed interactions in the intracellular region II. A hydrophobic contact network is shown in IIa. The van der Waals forces at the homodimer interface are shown in IIb. d Comparison of the dimeric interface of apo GPR156 transmembrane domains with those of apo GABA_B receptor (PDB code: 6VJM) and apo GPR158 (PDB code: 7EWL). e The basal activity of WT and versions with mutations in the dimer interface of GPR156, as measured by BRET-based assay (from left to right n = 8, 6, 7, 8, 8, 8, 8, 6, 6, 8, 6, 6, 6; D222^5.37A vs WT: P = 2.52817E-06; R279^6.57A vs WT: P = 0.5694; Y280^6.58A vs WT: P = 0.0560; V276^6.54A vs WT: P = 0.0118; V223^5.38A vs WT: P = 0.0006; L237^5.52A vs WT: P = 5.2657E-08; V264^6.42A vs WT: P = 0.0015; V268^6.46A vs WT: P = 0.0309; M261^6.39A vs WT: P = 3.1286E-07; Y241^5.56A vs WT: P = 0.0014; L234^5.49A vs WT: P = 6.6258E-06). Data are presented as a percentage of WT activity and are shown as the mean ± SEM (bars) from at least six independent experiments performed in technical triplicate with individual data points shown (dots). ns (not significant) = P > 0.05, *P < 0.05, **P < 0.01, ***P < 0.001, and ****P < 0.0001 by two-tailed unpaired t test compared to WT. Supplementary Fig. 7c provides the related surface expression level, and Supplementary Table 3 provides detailed information. Source data are provided as a Source Data file. f The key residues in the ionic lock motif (3.50 and 6.35) are aligned among members of class C GPCRs. g Close-up view of the conserved ionic lock motif showing the different conformations between GPR156 and other members of the class C subfamily in the apo state, including GABA_B receptor (PDB code: 6VJM) and GPR158 (PDB code: 7EWL).