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• W4297029789 abstract "Heterotrimeric G proteins (G proteins) are essential cellular signaling proteins that mediate extracellular signals to achieve various cellular functions. G-protein-coupled receptors (GPCRs) are the major guanine nucleotide exchange factors (GEFs) that induce G proteins to release guanosine diphosphate and rapidly bind to guanosine triphosphate, resulting in G protein activation. G proteins undergo dynamic conformational changes during the activation/inactivation process, and the precise structural mechanism of GPCR-mediated G protein activation is of great interest. Over the last decade, a number of GPCR-G protein complex structures have been identified, yet an understanding of the mechanisms underlying allosteric conformational changes during receptor-mediated G protein activation and GPCR-G protein coupling selectivity is only now emerging. This review discusses recent studies on the dynamic conformational changes of G proteins and provides insight into the structural mechanism of GPCR-mediated G protein activation.KeywordsGPCRG proteinConformational dynamicsSignaling selectivity" @default.
• W4297029789 created "2022-09-25" @default.
• W4297029789 creator A5003075346 @default.
• W4297029789 creator A5079184638 @default.
• W4297029789 date "2022-01-01" @default.
• W4297029789 modified "2023-09-29" @default.
• W4297029789 title "The Conformational Dynamics of Heterotrimeric G Proteins During GPCR-Mediated Activation" @default.
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• W4297029789 doi "https://doi.org/10.1007/978-3-031-00793-4_8" @default.
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