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Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser

文献类型：期刊论文

作者Kang, Yanyong3; Zhou, X. Edward3; Gao, Xiang3; He, Yuanzheng3; Liu, Wei4,5; Ishchenko, Andrii6; Barty, Anton7; Sathish, D.7; Yefanov, Oleksandr7; Han, Gye Won6
刊名NATURE
出版日期2015-07-30
卷号523期号:7562页码:561-+
ISSN号0028-0836
DOI10.1038/nature14656
文献子类Article
英文摘要G-protein-coupled receptors (GPCRs) signal primarily through G proteins or arrestins. Arrestin binding to GPCRs blocks G protein interaction and redirects signalling to numerous G-protein-independent pathways. Here we report the crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin, determined by serial femtosecond X-ray laser crystallography. Together with extensive biochemical and mutagenesis data, the structure reveals an overall architecture of the rhodopsin-arrestin assembly in which rhodopsin uses distinct structural elements, including transmembrane helix 7 and helix 8, to recruit arrestin. Correspondingly, arrestin adopts the pre-activated conformation, with a similar to 20 degrees rotation between the amino and carboxy domains, which opens up a cleft in arrestin to accommodate a short helix formed by the second intracellular loop of rhodopsin. This structure provides a basis for understanding GPCR-mediated arrestin-biased signalling and demonstrates the power of X-ray lasers for advancing the frontiers of structural biology.
WOS关键词PROTEIN-COUPLED RECEPTOR ; LIPIDIC CUBIC PHASE ; ROD OUTER SEGMENTS ; VISUAL ARRESTIN ; SEROTONIN RECEPTORS ; THERMAL-STABILITY ; MEMBRANE-PROTEINS ; SPACE-GROUP ; ACTIVATION ; BINDING
资助项目US Department of Energy, Office of Science, Office of Basic Energy Sciences[DE-AC02-76SF00515] ; National Institutes of Health[P41GM103393] ; Michigan Economic Development Corporation[00000000] ; Michigan Technology Tri-Corridor[085P1000817] ; Federal funds from the National Cancer Institute[ACB-12002] ; National Institute of General Medical Sciences[AGM-12006] ; Office of Science of the US Department of Energy[DE-AC02-06CH11357] ; Jay and Betty Van Andel Foundation, Ministry of Science and Technology (China)[2012ZX09301001] ; Jay and Betty Van Andel Foundation, Ministry of Science and Technology (China)[2012CB910403] ; Jay and Betty Van Andel Foundation, Ministry of Science and Technology (China)[2013CB910600] ; Jay and Betty Van Andel Foundation, Ministry of Science and Technology (China)[XDB08020303] ; Jay and Betty Van Andel Foundation, Ministry of Science and Technology (China)[2013ZX09507001] ; Amway (China)[00000000] ; National Institute of Health[DK071662] ; National Institute of Health[GM073197] ; National Institute of Health[GM103310] ; National Institute of Health[GM102545] ; National Institute of Health[GM104212] ; National Institute of Health[EY011500] ; National Institute of Health[GM077561] ; National Institute of Health[EY005216] ; National Institute of Health[P30EY000331] ; National Institutes of Health Common Fund in Structural Biology grants[P50 GM073197] ; National Institutes of Health Common Fund in Structural Biology grants[P50 GM073210] ; National Institutes of Health Common Fund in Structural Biology grants[GM095583] ; NSF Science and Technology Center[1231306] ; Swiss National Science Foundation[31003A_141235] ; Canada Excellence Research Chair program[00000000] ; Anne & Max Tanenbaum Chair in Neuroscience at the University of Toronto[00000000] ; Science Foundation Ireland[12/IA/1255] ; Helmholtz Gemeinschaft[00000000] ; DFG Cluster of Excellence Center for Ultrafast Imaging[00000000] ; BMBF[FKZ 05K12CH1] ; Irene and Eric Simon Brain Research Foundation[00000000] ; PIER Helmholtz-Graduate School[00000000] ; Helmholtz Association[00000000] ; National Institute of General Medical Sciences PSI: Biology grants[U54 GM094618] ; National Institute of General Medical Sciences PSI: Biology grants[GM108635] ; National Institute of General Medical Sciences PSI: Biology grants[U54 GM094599] ; National Institute of General Medical Sciences PSI: Biology grants[GM097463] ; National Institute of General Medical Sciences PSI: Biology grants[U54 GM094586]
WOS研究方向Science & Technology - Other Topics
语种英语
出版者NATURE PUBLISHING GROUP
WOS记录号WOS:000358655200038
源URL[http://119.78.100.183/handle/2S10ELR8/276463]  
专题药物靶标结构与功能中心
中科院受体结构与功能重点实验室
新药研究国家重点实验室
通讯作者Xu, H. Eric
作者单位1.Ctr Ultrafast Imaging, D-22761 Hamburg, Germany;
2.Chinese Acad Sci, Shanghai Inst Mat Med, CAS Key Lab Receptor Res, VARI SIMM Ctr,Ctr Struct & Funct Drug Targets, Shanghai 201203, Peoples R China
3.Van Andel Res Inst, Ctr Struct Biol & Drug Discovery, Lab Struct Sci, Grand Rapids, MI 49503 USA;
4.Arizona State Univ, Dept Chem & Biochem, Biodesign Inst, Tempe, AZ 85287 USA;
5.Arizona State Univ, Ctr Appl Struct Discovery, Biodesign Inst, Tempe, AZ 85287 USA;
6.Univ So Calif, Bridge Inst, Dept Chem, Los Angeles, CA 90089 USA;
7.Deutsch Elektronen Synchrotron DESY, Ctr Free Elect Laser Sci, D-22607 Hamburg, Germany;
8.SLAC Natl Accelerator Lab, Stanford Synchrotron Radiat Lightsource, Joint Ctr Struct Genom, Menlo Pk, CA 94025 USA;
9.Natl Univ Singapore, Yong Loo Lin Sch Med, Dept Obstet & Gynecol, Singapore 117595, Singapore;
10.New York Struct Biol Ctr, Natl Resource Automated Mol Microscopy, New York, NY 10027 USA;
推荐引用方式
GB/T 7714		 Kang, Yanyong,Zhou, X. Edward,Gao, Xiang,et al. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser[J]. NATURE,2015,523(7562):561-+.
APA Kang, Yanyong.,Zhou, X. Edward.,Gao, Xiang.,He, Yuanzheng.,Liu, Wei.,...&Xu, H. Eric.(2015).Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser.NATURE,523(7562),561-+.
MLA Kang, Yanyong,et al."Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser".NATURE 523.7562(2015):561-+.

入库方式： OAI收割

来源：上海药物研究所

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