Citation: Longmei Li, Jin Zhang, Wenjing Sun, Weimin Gong, Changlin Tian, Pan Shi, Chaowei Shi. Allosteric conformational changes of G proteins upon its interaction with membrane and GPCR[J]. Chinese Chemical Letters, ;2022, 33(2): 747-750. doi: 10.1016/j.cclet.2021.07.042 shu

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

Longmei Li ^{a, b} ,
Jin Zhang ^a ,
Wenjing Sun ^a ,
Weimin Gong ^a ,
Changlin Tian ^a ,
Pan Shi ^{a, *} ,
Chaowei Shi ^{a, *}

a.
Hefei National Laboratory of Physical Science at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China
b.
Department of Chemical Physics at School of Chemistry and Materials Sciences, University of Science and Technology of China, Hefei 230027, China

shipan@ustc.edu.cn

scwei@ustc.edu.cn

Received Date: 2 April 2021
Revised Date: 13 July 2021
Accepted Date: 15 July 2021
Available Online: 21 July 2021

Figures(4)

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 G_α in apo states. The interaction of G_α with detergents will accelerate this conformational transformation and induce a state that tends to bind to GPCRs. Finally, the G_α proteins presented a fully activation state when they coupled to GPCRs.
- ¹⁹F solution NMR,
- G protein-coupled receptors,
- Conformational dynamics,
- G protein
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