A genetically encoded small-size fluorescent pair reveals allosteric conformational changes of G proteins upon its interaction with GPCRs by fluorescence lifetime based FRET.

A genetically encoded small-size fluorescent pair reveals allosteric conformational changes of G proteins upon its interaction with GPCRs by fluorescence lifetime based FRET.
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DOI:
10.1039/d0cc02691c
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发表时间:
2020-05
影响因子:
4.9
通讯作者:
P. Shi;Yanan Zhang;P. Lv;W. Fang;S. Ling;Xiaoqi Guo;Dong Li;Sanling Liu;Demeng Sun;Long-hua Zhang;Dongsheng Liu;Ji‐Shen Zheng;C. Tian
P. Shi;Yanan Zhang;P. Lv;W. Fang;S. Ling;Xiaoqi Guo;Dong Li;Sanling Liu;Demeng Sun;Long-hua Zhang;Dongsheng Liu;Ji‐Shen Zheng;C. Tian
中科院分区:
化学2区
文献类型:
--
作者:
P. Shi;Yanan Zhang;P. Lv;W. Fang;S. Ling;Xiaoqi Guo;Dong Li;Sanling Liu;Demeng Sun;Long-hua Zhang;Dongsheng Liu;Ji‐Shen Zheng;C. Tian

文献摘要

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G蛋白偶联受体(GPCRs,G protein-coupled receptors)偶联G蛋白的动力学在信号转导中起着重要作用。本文报道了一种位点特异性标记的小分子荧光对7-HC/FlAsH((7-hydroxycoumarin-4-yl)-ethylglycine/fluorescein arsenical hairpin),用于基于荧光寿命的FRET(fluorescence resonance energy transfer),以揭示抑制性G蛋白Gα i 1和刺激性G蛋白Gαs在β 2 AR(β2-adrenergic receptor)偶联后的构象差异。它提供了一种新的普遍适用的方法来探测蛋白质的动态相互作用或构象变化。
The dynamics of GPCRs (G protein-coupled receptors) coupling for cognate G proteins play a critical role in signal transduction. Herein, we reported a site-specifically labelled small-sized fluorescent pair 7-HC/FlAsH ((7-hydroxycoumarin-4-yl)-ethylglycine/fluorescein arsenical hairpin) for fluorescence lifetime based FRET (fluorescence resonance energy transfer) to reveal conformational differences of Gαi1 (inhibitory G proteins) and Gαs (stimulatory G proteins) upon β2AR (β2-adrenergic receptor) coupling. It offers a new generally applicable method to probe protein dynamic interactions or conformational changes.