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Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
Kang, YY; Zhou, XE; Gao, X; He, YZ; Liu, W; Ishchenko, A; Barty, A; Sathish, D; Yefanov, O; Han, GW; Xu, QP; de Waal, PW; Ke, JY; Tan, MHE; Zhang, CH; Moeller, A; West, GM; Pascal, BD; Van Eps, N; Caro, LN; Vishnivetskiy, SA; Lee, RJ; Suino-Powell, KM; Gu, X; Pal, K; Ma, JM; Zhi, XY; Boutet, S; Williams, GJ; Messerschmidt, M; Gati, C; Zatsepin, NA; Wang, DJ; James, D; Basu, S; Roy-Chowdhury, S; Conrad, CE; Coe, J; Liu, HG; Lisova, S; Kupitz, C; Grotjohann, I; Fromme, R; Jiang, Y; Tan, MJ; Yang, HY; Li, J; Wang, MT; Zheng, Z; Li, DF; Howe, N; Zhao, YM; Standfuss, J; Diederichs, K; Dong, YH; Potter, CS; Carragher, B; Caffrey, M; Jiang, HL; Chapman, HN; Spence, JCH; Fromme, P; Weierstall, U; Ernst, OP; Katritch, V; Gurevich, VV; Griffin, PR; Hubbell, WL; Stevens, RC; Cherezov, V; Melcher, K; Xu, HE; Dong YH(董宇辉)
2015
发表期刊NATURE
卷号523期号:7562页码:561-567
文章类型Article
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.
学科领域Science & Technology - Other Topics
DOI10.1038/nature14656
收录类别SCI
WOS类目Multidisciplinary Sciences
WOS记录号WOS:000358655200038
引用统计
被引频次:259[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/228576
专题多学科研究中心
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Kang, YY,Zhou, XE,Gao, X,et al. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser[J]. NATURE,2015,523(7562):561-567.
APA Kang, YY.,Zhou, XE.,Gao, X.,He, YZ.,Liu, W.,...&董宇辉.(2015).Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser.NATURE,523(7562),561-567.
MLA Kang, YY,et al."Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser".NATURE 523.7562(2015):561-567.
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