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Zhang, Meng; Gui, Miao; Wang, Zi-Fu; Gorgulla, Christoph; Yu, James J; Wu, Hao; Sun, Zhen-Yu J; Klenk, Christoph; Merklinger, Lisa; Morstein, Lena; Hagn, Franz; Plückthun, Andreas; Brown, Alan; Nasr, Mahmoud L; Wagner, Gerhard
Nature structural & molecular biology, 03/2021, Volume: 28, Issue: 3Journal Article
G-protein-coupled receptors (GPCRs) are the largest superfamily of transmembrane proteins and the targets of over 30% of currently marketed pharmaceuticals. Although several structures have been solved for GPCR-G protein complexes, few are in a lipid membrane environment. Here, we report cryo-EM structures of complexes of neurotensin, neurotensin receptor 1 and Gα β γ in two conformational states, resolved to resolutions of 4.1 and 4.2 Å. The structures, determined in a lipid bilayer without any stabilizing antibodies or nanobodies, reveal an extended network of protein-protein interactions at the GPCR-G protein interface as compared to structures obtained in detergent micelles. The findings show that the lipid membrane modulates the structure and dynamics of complex formation and provide a molecular explanation for the stronger interaction between GPCRs and G proteins in lipid bilayers. We propose an allosteric mechanism for GDP release, providing new insights into the activation of G proteins for downstream signaling.
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