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
Structural and Functional Characterization of Ryanodine Receptor-Natrin Toxin Interaction
Zhou, Qiang2; Wang, Qiong-Ling3; Meng, Xing1; Shu, Yuyan4; Jiang, Tao5; Wagenknecht, Terence1,6; Yin, Chang-Cheng3; Sui, Sen-Fang2; Liu, Zheng1
刊名BIOPHYSICAL JOURNAL
2008-11-01
DOI10.1529/biophysj.108.137224
95期:9页:4289-4299
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biophysics
研究领域[WOS]Biophysics
关键词[WOS]RICH SECRETORY PROTEIN ; CALCIUM-RELEASE CHANNEL ; MUSCLE SARCOPLASMIC-RETICULUM ; GATED ION CHANNELS ; SKELETAL-MUSCLE ; SNAKE-VENOM ; CRYOELECTRON MICROSCOPY ; CRYSTAL-STRUCTURE ; 3-DIMENSIONAL RECONSTRUCTION ; INTERDOMAIN INTERACTIONS
英文摘要

Cysteine-rich secretory proteins (CRISPs) are widely distributed, and notably occur in the mammalian reproductive tract and in the salivary glands of venomous reptiles. Most CRISPs can inhibit ion channels, such as the cyclic nucleotide-gated ion channel, potassium channel, and calcium channel. Natrin is a CRISP that has been purified from snake venom. Its targets include the calcium-activated potassium channel, the voltage-gated potassium channel, and the calcium release channel/ryanodine receptor (RyR). Immunoprecipitation experiments showed that natrin binds specifically to type 1 RyR (RyR1) from skeletal muscle. Natrin was found to inhibit both the binding of ryanodine to RyR1, and the calcium-channel activity of RyR1. Cryo-electron microscopy and single-particle image reconstruction analysis revealed that natrin binds to the clamp domains of RyR1. Docking of the crystal structure of natrin into our cryo-electron microscopy density map of the RyR1 + natrin complex suggests that natrin inhibits RyR1 by stabilizing a domain-domain interaction, and that the cysteine-rich domain of natrin is crucial for binding. These findings help reveal how natrin toxin inhibits the RyR calcium release channel, and they allow us to posit a generalized mechanism that governs the interaction between CRISPs and ion channels.

语种英语
WOS记录号WOS:000260072600022
项目编号0430076N ; AR40615 ; 30330160 ; 30370379 ; 2004CB720005
资助机构American Heart Association ; National Institutes of Health ; Natural Science Foundation of China ; Trans-Century Talent-Awarding Program ; Ministry of Education, China ; National Basic Research Program of China
引用统计
被引频次:23[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/400002259/51360
专题北京大学基础医学院_生物物理学系
作者单位1.Wadsworth Ctr, New York State Dept Hlth, Albany, NY 12201 USA
2.Tsinghua Univ, Dept Biol Sci & Biotechnol, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
3.Peking Univ, Hlth Sci Ctr, Dept Biophys, Beijing 100191, Peoples R China
4.Guangxi Med Univ, Snake Venom Res Inst, Nanning 530021, Guangxi, Peoples R China
5.Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China
6.SUNY Albany, Sch Publ Hlth, Dept Biomed Sci, Albany, NY 12201 USA
推荐引用方式
GB/T 7714
Zhou, Qiang,Wang, Qiong-Ling,Meng, Xing,et al. Structural and Functional Characterization of Ryanodine Receptor-Natrin Toxin Interaction[J]. BIOPHYSICAL JOURNAL,2008,95(9):4289-4299.
APA Zhou, Qiang.,Wang, Qiong-Ling.,Meng, Xing.,Shu, Yuyan.,Jiang, Tao.,...&Liu, Zheng.(2008).Structural and Functional Characterization of Ryanodine Receptor-Natrin Toxin Interaction.BIOPHYSICAL JOURNAL,95(9),4289-4299.
MLA Zhou, Qiang,et al."Structural and Functional Characterization of Ryanodine Receptor-Natrin Toxin Interaction".BIOPHYSICAL JOURNAL 95.9(2008):4289-4299.
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