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.
复制标题
DOI:
10.1039/d0cc02691c
复制
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
中科院分区:
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
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.