Literature DB >> 31102356

[Single-particle cryo-electron microscopy opens new avenues in structural biology of G protein-coupled receptor].

Chuntao Li1, Huibing Zhang1, Yan Zhang1,2.   

Abstract

G protein-coupled receptors(GPCRs)represent the largest class of cell surface receptors,mediating wide range of cellular and physiological processes through their transducers,G proteins and the-arrestins participate in almost all pathological processes. Recent technological advances are revolutionizing the utility of cryo-electron microscopy(cryo-EM),leading to a tremendous progress in the structural studies of biological macromolecules and cryo-EM has played a leading role in the structural biology of GPCR signaling complex. New discoveries of high-resolution threedimensional structures of GPCR signaling complexes based on cryo-EM have emerged vigorously,which depict the common structural characteristics of intermolecular interaction between GPCR and G protein complex-the conformational changes of the transmembrane helix 6 of receptors,and also demonstrate the structural basis of G protein subtype selectivity. Single-particle cryo-EM becomes an efficient tool for identifying the molecular mechanism of receptor-ligand interaction,providing important information for understanding GPCR signaling and the structure-based drug design.

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Year:  2019        PMID: 31102356      PMCID: PMC8800651          DOI: 10.3785/j.issn.1008-9292.2019.02.07

Source DB:  PubMed          Journal:  Zhejiang Da Xue Xue Bao Yi Xue Ban        ISSN: 1008-9292


  19 in total

Review 1.  Methodological advances: the unsung heroes of the GPCR structural revolution.

Authors:  Eshan Ghosh; Punita Kumari; Deepika Jaiman; Arun K Shukla
Journal:  Nat Rev Mol Cell Biol       Date:  2015-01-15       Impact factor: 94.444

2.  Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis.

Authors:  Thomas J Cahill; Alex R B Thomsen; Jeffrey T Tarrasch; Bianca Plouffe; Anthony H Nguyen; Fan Yang; Li-Yin Huang; Alem W Kahsai; Daniel L Bassoni; Bryant J Gavino; Jane E Lamerdin; Sarah Triest; Arun K Shukla; Benjamin Berger; John Little; Albert Antar; Adi Blanc; Chang-Xiu Qu; Xin Chen; Kouki Kawakami; Asuka Inoue; Junken Aoki; Jan Steyaert; Jin-Peng Sun; Michel Bouvier; Georgios Skiniotis; Robert J Lefkowitz
Journal:  Proc Natl Acad Sci U S A       Date:  2017-02-21       Impact factor: 11.205

3.  Structure of the adenosine-bound human adenosine A1 receptor-Gi complex.

Authors:  Christopher J Draper-Joyce; Maryam Khoshouei; David M Thal; Yi-Lynn Liang; Anh T N Nguyen; Sebastian G B Furness; Hariprasad Venugopal; Jo-Anne Baltos; Jürgen M Plitzko; Radostin Danev; Wolfgang Baumeister; Lauren T May; Denise Wootten; Patrick M Sexton; Alisa Glukhova; Arthur Christopoulos
Journal:  Nature       Date:  2018-06-20       Impact factor: 49.962

4.  Publisher Correction: Cryo-EM structure of human rhodopsin bound to an inhibitory G protein.

Authors:  Yanyong Kang; Oleg Kuybeda; Parker W de Waal; Somnath Mukherjee; Ned Van Eps; Przemyslaw Dutka; X Edward Zhou; Alberto Bartesaghi; Satchal Erramilli; Takefumi Morizumi; Xin Gu; Yanting Yin; Ping Liu; Yi Jiang; Xing Meng; Gongpu Zhao; Karsten Melcher; Oliver P Ernst; Anthony A Kossiakoff; Sriram Subramaniam; H Eric Xu
Journal:  Nature       Date:  2018-09       Impact factor: 49.962

5.  Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptor-Gs complex.

Authors:  Yi-Lynn Liang; Maryam Khoshouei; Alisa Glukhova; Sebastian G B Furness; Peishen Zhao; Lachlan Clydesdale; Cassandra Koole; Tin T Truong; David M Thal; Saifei Lei; Mazdak Radjainia; Radostin Danev; Wolfgang Baumeister; Ming-Wei Wang; Laurence J Miller; Arthur Christopoulos; Patrick M Sexton; Denise Wootten
Journal:  Nature       Date:  2018-02-21       Impact factor: 49.962

6.  X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis.

Authors:  J Deisenhofer; O Epp; K Miki; R Huber; H Michel
Journal:  J Mol Biol       Date:  1984-12-05       Impact factor: 5.469

7.  Crystal structure of the β2 adrenergic receptor-Gs protein complex.

Authors:  Søren G F Rasmussen; Brian T DeVree; Yaozhong Zou; Andrew C Kruse; Ka Young Chung; Tong Sun Kobilka; Foon Sun Thian; Pil Seok Chae; Els Pardon; Diane Calinski; Jesper M Mathiesen; Syed T A Shah; Joseph A Lyons; Martin Caffrey; Samuel H Gellman; Jan Steyaert; Georgios Skiniotis; William I Weis; Roger K Sunahara; Brian K Kobilka
Journal:  Nature       Date:  2011-07-19       Impact factor: 49.962

8.  Functional competence of a partially engaged GPCR-β-arrestin complex.

Authors:  Punita Kumari; Ashish Srivastava; Ramanuj Banerjee; Eshan Ghosh; Pragya Gupta; Ravi Ranjan; Xin Chen; Bhagyashri Gupta; Charu Gupta; Deepika Jaiman; Arun K Shukla
Journal:  Nat Commun       Date:  2016-11-09       Impact factor: 14.919

9.  Phase-plate cryo-EM structure of a class B GPCR-G-protein complex.

Authors:  Yi-Lynn Liang; Maryam Khoshouei; Mazdak Radjainia; Yan Zhang; Alisa Glukhova; Jeffrey Tarrasch; David M Thal; Sebastian G B Furness; George Christopoulos; Thomas Coudrat; Radostin Danev; Wolfgang Baumeister; Laurence J Miller; Arthur Christopoulos; Brian K Kobilka; Denise Wootten; Georgios Skiniotis; Patrick M Sexton
Journal:  Nature       Date:  2017-04-24       Impact factor: 49.962

10.  Cryo-EM structure of the adenosine A2A receptor coupled to an engineered heterotrimeric G protein.

Authors:  Javier García-Nafría; Yang Lee; Xiaochen Bai; Byron Carpenter; Christopher G Tate
Journal:  Elife       Date:  2018-05-04       Impact factor: 8.140

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