摘要
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 ^(19)F 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.
基金
supported by the National Key Research and Development Project of China (Nos.2019YFA0904100 and 2017YFA0505400)
the National Natural Science Foundation of China (Nos.22077117 and 31971152)
the USTC Research Funds of the Double First-Class Initiative。
