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.
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Acknowledgments
This work was supported by the National Research Foundation of Korea and funded by the Ministry of Science and ICT of Korea (NRF-2021R1A2C3003518) and under the framework of the international cooperation program managed by the National Research Foundation of Korea (NRF-2021K2A9A2A08000144).
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Ahn, D., Chung, K.Y. (2022). The Conformational Dynamics of Heterotrimeric G Proteins During GPCR-Mediated Activation. In: Harris, J.R., Marles-Wright, J. (eds) Macromolecular Protein Complexes IV. Subcellular Biochemistry, vol 99. Springer, Cham. https://doi.org/10.1007/978-3-031-00793-4_8
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