New insights into GPCR coupling and dimerisation from cryo-EM structures

被引：24

作者：

Gusach, Anastasiia ^{[1
]}

Garcia-Nafria, Javier ^{[2
,3
]}

Tate, Christopher G. ^{[1
]}

机构：

[1] MRC, Lab Mol Biol, Francis Crick Ave, Cambridge CB2 2QH, England

[2] Univ Zaragoza, Inst Biocomputat & Phys Complex Syst BIFI, Zaragoza 50018, Spain

[3] Univ Zaragoza, Lab Microscopias Avanzadas LMA, Zaragoza 50018, Spain

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2023年 / 80卷

基金：

英国医学研究理事会;

关键词：

STABILIZED ACTIVE STATE; PROTEIN; ACTIVATION; ARRESTIN; RECOGNITION; RHODOPSIN; MECHANISM;

D O I：

10.1016/j.sbi.2023.102574

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Over the past three years (2020-2022) more structures of GPCRs have been determined than in the previous twenty years (2000-2019), primarily of GPCR complexes that are large enough for structure determination by single-particle cryo-EM. This review will present some structural highlights that have advanced our molecular understanding of promiscuous G protein coupling, how a G protein receptor kinase and L-arrestins couple to GPCRs, and GPCR dimerisation. We will also discuss advances in the use of gene fusions, nanobodies, and Fab fragments to facilitate the structure determination of GPCRs in the inactive state that, on their own, are too small for structure determination by single-particle cryo-EM.

引用

页数：10

共 50 条

[21] Cryo-EM structures of lentiviral intasomes
Cherepanov, P.
FEBS OPEN BIO, 2018, 8 : 32 - 32
[22] A homotrimeric GPCR architecture of the human cytomegalovirus revealed by cryo-EM
Chen, Yanyan
Li, Yang
Zhou, Qingtong
Cong, Zhaotong
Lin, Shi
Yan, Jiahui
Chen, Xianyue
Yang, Dehua
Ying, Tianlei
Wang, Ming-Wei
CELL DISCOVERY, 2024, 10 (01)
[23] Evolving cryo-EM structural approaches for GPCR drug discovery
Zhang, Xin
Johnson, Rachel M.
Drulyte, Ieva
Yu, Lingbo
Kotecha, Abhay
Danev, Radostin
Wootten, Denise
Sexton, Patrick M.
Belousoff, Matthew J.
STRUCTURE, 2021, 29 (09) : 963 - +
[24] Insights into homology search from cryo-EM structures of RecA-DNA recombination intermediates
Yang, Haijuan
Pavletich, Nikola P.
CURRENT OPINION IN GENETICS & DEVELOPMENT, 2021, 71 : 188 - 194
[25] Cryo-EM structures and biochemical insights into heterotrimeric PCNA regulation of DNA ligase
Sverzhinsky, Aleksandr
Tomkinson, Alan E.
Pascal, John M.
STRUCTURE, 2022, 30 (03) : 371 - +
[26] Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria
Tan, Yong Zi
Zhang, Lei
Rodrigues, Jose
Zheng, Ruixiang Blake
Giacometti, Sabrina, I
Rosario, Ana L.
Kloss, Brian
Dandey, Venkata P.
Wei, Hui
Brunton, Richard
Raczkowski, Ashleigh M.
Athayde, Diogo
Catalao, Maria Joao
Pimentel, Madalena
Clarke, Oliver B.
Lowary, Todd L.
Archer, Margarida
Niederweis, Michael
Potter, Clinton S.
Carragher, Bridget
Mancia, Filippo
MOLECULAR CELL, 2020, 78 (04) : 683 - +
[27] From cryo-EM, multiple protein structures in one shot
Sigworth, Fred J.
NATURE METHODS, 2007, 4 (01) : 20 - 21
[28] From cryo-EM, multiple protein structures in one shot
Fred J Sigworth
Nature Methods, 2007, 4 : 20 - 21
[29] Cryo-EM enters a new era
Kuehlbrandt, Werner
ELIFE, 2014, 3
[30] Validation, analysis and annotation of cryo-EM structures
Pintilie, Grigore
Chiu, Wah
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2021, 77 : 1142 - 1152

← 1 2 3 4 5 →