A genetically encoded small-size fluorescent pair reveals allosteric conformational changes of G proteins upon its interaction with GPCRs by fluorescence lifetime based FRET-Reference-Cited by-同舟云学术

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

Published:2020 Issue:51 Volume:56 Page:6941-6944
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Shi Pan¹²³⁴,Zhang Yanan¹²³⁴,Lv Pei¹²³⁴,Fang Wei¹²³⁴,Ling Shenglong¹²³⁴,Guo Xiaoqi¹²³⁴,Li Dong¹²³⁴,Liu Sanling¹²³⁴,Sun Demeng¹²³⁴,Zhang Longhua¹²³⁴,Liu Dongsheng⁵⁶⁷⁸,Zheng Ji-Shen¹²³⁴^ORCID,Tian Changlin¹²³⁴⁹^ORCID

Affiliation:

1. Hefei National Laboratory of Physical Science at Microscale and School of Life Sciences

2. University of Science and Technology of China

3. Hefei

4. P. R. China

5. iHuman Institute

6. ShanghaiTech University

7. Shanghai

8. China

9. High Magnetic Field Laboratory

Abstract

A genetically encoded small-size fluorescent pair to reveal the conformational changes of G proteins upon binding GPCRs by fluorescence lifetime based FRET.

Funder

National Natural Science Foundation of China

National Basic Research Program of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2020/CC/D0CC02691C

Reference26 articles.

1. Molecular mechanism of biased signaling in a prototypical G protein–coupled receptor

2. Angiotensin and biased analogs induce structurally distinct active conformations within a GPCR

3. Crystal structure of the β2 adrenergic receptor–Gs protein complex

4. Structures of the M1 and M2 muscarinic acetylcholine receptor/G-protein complexes

5. Structure of the neurotensin receptor 1 in complex with β-arrestin 1

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