Structural insights into ca2+-activated long-range allosteric channel gating of ryr1 | |
Wei, Risheng1; Wang, Xue2,3; Zhang, Yan2; Mukherjee, Saptarshi4; Zhang, Lei1,5; Chen, Qiang1; Huang, Xinrui1; Jing, Shan1; Liu, Congcong1; Li, Shuang1 | |
刊名 | Cell research |
2016-09-01 | |
卷号 | 26期号:9页码:977-994 |
关键词 | Ca2+ activation Cryo-electron microscopy Channel gating Ion selectivity Long-range allostery Ryanodine receptor Single-particle analysis |
ISSN号 | 1001-0602 |
DOI | 10.1038/cr.2016.99 |
通讯作者 | Sun, fei(feisun@ibp.ac.cn) ; Yin, chang-cheng(ccyin@hsc.pku.edu.cn) |
英文摘要 | Ryanodine receptors (ryrs) are a class of giant ion channels with molecular mass over 2.2 mega-daltons. these channels mediate calcium signaling in a variety of cells. since more than 80% of the ryr protein is folded into the cytoplasmic assembly and the remaining residues form the transmembrane domain, it has been hypothesized that the activation and regulation of ryr channels occur through an as yet uncharacterized long-range allosteric mechanism. here we report the characterization of a ca2+-activated open-state ryr1 structure by cryo-electron microscopy. the structure has an overall resolution of 4.9 angstrom and a resolution of 4.2 angstrom for the core region. in comparison with the previously determined apo/closed-state structure, we observed long-range allosteric gating of the channel upon ca2+ activation. in-depth structural analyses elucidated a novel channel-gating mechanism and a novel ion selectivity mechanism of ryr1. our work not only provides structural insights into the molecular mechanisms of channel gating and regulation of ryrs, but also sheds light on structural basis for channel-gating and ion selectivity mechanisms for the six-transmembrane-helix cation channel family. |
WOS关键词 | CALCIUM-RELEASE CHANNEL ; MUSCLE RYANODINE RECEPTOR ; EM STRUCTURE DETERMINATION ; AMINO-ACID-RESIDUES ; PARTICLE CRYO-EM ; C-TERMINAL TAIL ; SKELETAL-MUSCLE ; SARCOPLASMIC-RETICULUM ; ELECTRON CRYOMICROSCOPY ; CARDIAC-MUSCLE |
WOS研究方向 | Cell Biology |
WOS类目 | Cell Biology |
语种 | 英语 |
出版者 | INST BIOCHEMISTRY & CELL BIOLOGY |
WOS记录号 | WOS:000382398100005 |
内容类型 | 期刊论文 |
URI标识 | http://www.corc.org.cn/handle/1471x/2375716 |
专题 | 中国科学院大学 |
通讯作者 | Sun, Fei; Yin, Chang-Cheng |
作者单位 | 1.Peking Univ, Dept Biophys, Hlth Sci Ctr, Beijing 100191, Peoples R China 2.Chinese Acad Sci, Inst Biophys, CAS Ctr Excellence Biomacromol, Natl Lab Biomacromol, Beijing 100101, Peoples R China 3.Univ Chinese Acad Sci, Coll Life Sci, Beijing 100049, Peoples R China 4.Cardiff Univ, Wales Heart Res Inst, Sch Med, Cardiff CF14 4XN, S Glam, Wales 5.Peking Univ, Hlth Sci Ctr, Electron Microscopy Anal Lab, Beijing 100191, Peoples R China 6.Chinese Acad Sci, Inst Biophys, Ctr Biol Imaging, Beijing 100101, Peoples R China 7.Peking Univ, Ctr Prot Sci, Beijing 100871, Peoples R China |
推荐引用方式 GB/T 7714 | Wei, Risheng,Wang, Xue,Zhang, Yan,et al. Structural insights into ca2+-activated long-range allosteric channel gating of ryr1[J]. Cell research,2016,26(9):977-994. |
APA | Wei, Risheng.,Wang, Xue.,Zhang, Yan.,Mukherjee, Saptarshi.,Zhang, Lei.,...&Yin, Chang-Cheng.(2016).Structural insights into ca2+-activated long-range allosteric channel gating of ryr1.Cell research,26(9),977-994. |
MLA | Wei, Risheng,et al."Structural insights into ca2+-activated long-range allosteric channel gating of ryr1".Cell research 26.9(2016):977-994. |
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