Matches in SemOpenAlex for { <https://semopenalex.org/work/W3034809991> ?p ?o ?g. }
- W3034809991 abstract "Abstract G protein coupled receptors (GPCRs) are the largest superfamily of transmembrane proteins and the targets of over 30% of currently marketed pharmaceuticals 1,2 . Although several structures have been solved for GPCR-G protein complexes 3–17 , structural studies of the complex in a physiological lipid membrane environment are lacking. Additionally, most previous studies required additional antibodies/nanobodies and/or engineered G proteins for complex stabilization. In the absence of a native complex structure, the underlying mechanism of G protein activation leading to GDP/GTP exchange remains unclear. Here, we report cryo-EM structures of lipid bilayer-bound complexes of neurotensin, neurotensin receptor 1, and Gα i1 β 1 γ 1 protein in two conformational states, resolved to 4.1 and 4.2 Å resolution. The structures were determined without any stabilizing antibodies/nanobodies, and thus provide a native-like platform for understanding the structural basis of GPCR-G protein complex formation. Our structures reveal an extended network of protein-protein interactions at the GPCR-G protein interface compared to in detergent micelles, defining roles for the lipid membrane in modulating the structure and dynamics of complex formation, and providing a molecular explanation for the stronger interaction between GPCR and G protein in lipid bilayers. We propose a detailed allosteric mechanism for GDP release, providing new insights into the activation of G proteins for downstream signaling under near native conditions." @default.
- W3034809991 created "2020-06-19" @default.
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- W3034809991 date "2020-06-12" @default.
- W3034809991 modified "2023-09-27" @default.
- W3034809991 title "Cryo-EM structure of an activated GPCR-G protein complex in lipid nanodiscs" @default.
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- W3034809991 doi "https://doi.org/10.1101/2020.06.11.145912" @default.
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