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. 2023 Aug 17;14:5004. doi: 10.1038/s41467-023-40705-z

Fig. 5. The coupling of MRPGRX1 with Gi1 and Gq.

Fig. 5

a Three-dimensional (3D) representation of the detailed interactions between MRGPRX1 and the α5-helix of Gαi. b Three-dimensional (3D) representation of the detailed interactions between MRGPRX1 and the α5-helix of Gαq. c Comparison of the Gi1/Gq coupling interfaces in cryo-EM structures of BAM8-22-MRGPRX1-Gq, BAM8-22-MRGPRX1-Gi1 and PAMP-12-MRGPRX2-Gi1 complexes. Residues of MRGPRX1 in contact with Gi1/Gq were illustrated as green dots. d Effects of mutations in the MRGPRX1 along the Gi trimer interface on BAM8-22 induced Gαi-Gγ dissociation. Statistical differences between WT and mutations were determined by two-sided one-way ANOVA with the Tukey test. *P  <  0.05; **P  <  0.01; ***P  <  0.001, ns, no significant difference. (P = 0.0109, 0.0091, ND, ND, ND, 0.1196, <0.001, ND from top to bottom). Data from three independent experiments are presented as the mean ± SEM (n = 3). e The structural representation and comparison of the interfaces between the MRGPRX1-Gi and MRGPRX1-Gq complexes. Ribbon representation: MRGPRX1 bound to Gi is shown in cornflower blue, MRGPRX1 bound to Gq is shown in salmon, Gi is shown in dark orange, Gq is shown in green. f Effects of mutations in the MRGPRX1 along the Gαq trimer interface on BAM8-22 induced Gαq-Gγ protein dissociation. Statistical differences between WT and mutations were determined by two-sided one-way ANOVA with the Tukey test. *P  <  0.05; **P  <  0.01; ***P  <  0.001, ns, no significant difference. (P  = 0.0003, <0.001, <0.0004,  <0.001, <0.001, <0.001, <0.001, P  <  0.001, ND, ND, <0.0001 from top to bottom) Data from three independent experiments are presented as the mean ± SEM (n = 3).