典型文献
Allosteric conformational changes of G proteins upon its interaction with membrane and GPCR
文献摘要：
Current resolved structures of GPCRs and G protein complexes provided important insights into G pro-tein 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 ad-dressed.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.
文献关键词：
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作者姓名：
Longmei Li;Jin Zhang;Wenjing Sun;Weimin Gong;Changlin Tian;Pan Shi;Chaowei Shi
作者机构：
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
文献出处：
引用格式：
[1]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].中国化学快报（英文版）,2022(02):747-750
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0.587334
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