Allosteric conformational changes of G proteins upon its interaction with membrane and GPCR

• Published in: Chinese chemical letters Vol. 33; no. 2; pp. 747 - 750
• Main Authors: Li, Longmei, Zhang, Jin, Sun, Wenjing, Gong, Weimin, Tian, Changlin, Shi, Pan, Shi, Chaowei
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.02.2022; Hefei National Laboratory of Physical Science at Microscale and School of Life Sciences,University of Science and Technology of China,Hefei 230027,China; Department of Chemical Physics at School of Chemistry and Materials Sciences,University of Science and Technology of China,Hefei 230027,China%Hefei National Laboratory of Physical Science at Microscale and School of Life Sciences,University of Science and Technology of China,Hefei 230027,China
• Subjects: 19F solution NMR; Conformational dynamics; G protein; G protein-coupled receptors; G protein-coupled receptors; 19F solution NMR; Conformational dynamics; G protein
• ISSN: 1001-8417; 1878-5964
• DOI: 10.1016/j.cclet.2021.07.042

Current resolved structures of GPCRs and G protein complexes provided important insights into G protein activation. However, the binding or dissociation of GPCRs with G protein is instantaneous and highly dynamic in the intracellular environment. The conformational dynamic of G protein still needs to be addressed. In this study, we applied 19F solution NMR spectroscopy to monitor the conformational changes of G protein upon interact with detergent mimicking membrane and receptor. Our results show that there are two states equilibria in the Gα in apo states. The interaction of Gα with detergents will accelerate this conformational transformation and induce a state that tends to bind to GPCRs. Finally, the Gα proteins presented a fully activation state when they coupled to GPCRs. 19F solution nuclear magnetic resonance (NMR) spectroscopy was applied to monitor the conformational dynamic changes of G protein upon interact with detergent mimicking membrane and β2AR, and the four states of G protein were successfully captured. [Display omitted]