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

查看全文 作　　者：Longmei [1,2]Li;Jin [1]Zhang;Wenjing [1]Sun;Weimin [1]Gong;Changlin [1]Tian;Pan [1]Shi;Chaowei [1]Shi

机构地区：[1]Hefei National Laboratory of Physical Science at Microscale and School of Life Sciences,University of Science and Technology of China,Hefei 230027,China;[2]Department of Chemical Physics at School of Chemistry and Materials Sciences,University of Science and Technology of China,Hefei 230027,China

出　　处：《Chinese Chemical Letters》索引2022年第33卷第2期,共4页

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。 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. 关键词：19F solution NMR G protein-coupled receptors Conformational dynamics G protein

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

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