IR@PKUHSC  > 北京大学基础医学院  > 生物物理学系
学科主题基础医学
Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution
Yan, Zhen1,2,3,4; Bai, Xiao-chen5; Yan, Chuangye2,3,4; Wu, Jianping2,3,4; Li, Zhangqiang1,2,4; Xie, Tian2,3,4; Peng, Wei1,2,4; Yin, Chang-cheng6,7; Li, Xueming2,4; Scheres, Sjors H. W.5; Shi, Yigong2,3,4; Yan, Nieng1,2,4
刊名NATURE
2015
DOI10.1038/nature14063
517期:7532页:50-+
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Multidisciplinary Sciences
研究领域[WOS]Science & Technology - Other Topics
关键词[WOS]CALCIUM-RELEASE CHANNEL ; PARTICLE ELECTRON CRYOMICROSCOPY ; MUSCLE SARCOPLASMIC-RETICULUM ; PORE-FORMING SEGMENT ; SKELETAL-MUSCLE ; CRYO-EM ; CRYOELECTRON MICROSCOPY ; TRANSMEMBRANE DOMAINS ; CRYSTAL-STRUCTURES ; CARDIAC-MUSCLE
英文摘要

The ryanodine receptors (RyRs) are high-conductance intracellular Ca2+ channels that play a pivotal role in the excitation-contraction coupling of skeletal and cardiac muscles. RyRs are the largest known ion channels, with a homotetrameric organization and approximately 5,000 residues in each protomer. Here we report the structure of the rabbit RyR1 in complex with its modulator FKBP12 at an overall resolution of 3.8 angstrom, determined by single-particle electron cryomicroscopy. Three previously uncharacterized domains, named central, handle and helical domains, display the armadillo repeat fold. These domains, together with the amino-terminal domain, constitute a network of superhelical scaffold for binding and propagation of conformational changes. The channel domain exhibits the voltage-gated ion channel superfamily fold with distinct features. A negative-charge-enriched hairpin loop connecting S5 and the pore helix is positioned above the entrance to the selectivity-filter vestibule. The four elongated S6 segments form a right-handed helical bundle that closes the pore at the cytoplasmic border of the membrane. Allosteric regulation of the pore by the cytoplasmic domains is mediated through extensive interactions between the central domains and the channel domain. These structural features explain high ion conductance by RyRs and the long-range allosteric regulation of channel activities.

语种英语
WOS记录号WOS:000347178400032
项目编号2015CB910101 ; 2011CB910501 ; 2014ZX09507003006 ; 31321062 ; 31130002 ; 31125009 ; MC_UP_A025_1013
资助机构Ministry of Science and Technology of China ; National Natural Science Foundation of China ; European Union ; UK Medical Research Council
引用统计
被引频次:164[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/66382
专题北京大学基础医学院_生物物理学系
作者单位1.Tsinghua Univ, Sch Med, Beijing 100084, Peoples R China
2.MRC Lab Mol Biol, Cambridge CB2 0QH, England
3.Peking Univ, Ctr Prot Sci, Beijing 100191, Peoples R China
4.Tsinghua Univ, Sch Life Sci, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
5.Tsinghua Univ, Sch Life Sci, Ministry Educ Key Lab Prot Sci, Beijing 100084, Peoples R China
6.Tsinghua Univ, Sch Life Sci, Ctr Struct Biol, Tsinghua Peking Joint Ctr Life Sci, Beijing 100084, Peoples R China
7.Peking Univ, Dept Biophys, Hlth Sci Ctr, Beijing 100191, Peoples R China
推荐引用方式
GB/T 7714
Yan, Zhen,Bai, Xiao-chen,Yan, Chuangye,et al. Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution[J]. NATURE,2015,517(7532):50-+.
APA Yan, Zhen.,Bai, Xiao-chen.,Yan, Chuangye.,Wu, Jianping.,Li, Zhangqiang.,...&Yan, Nieng.(2015).Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution.NATURE,517(7532),50-+.
MLA Yan, Zhen,et al."Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution".NATURE 517.7532(2015):50-+.
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