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学科主题: 基础医学
题名:
Structural and Functional Characterization of Ryanodine Receptor-Natrin Toxin Interaction
作者: 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
发表日期: 2008-11-01
DOI: 10.1529/biophysj.108.137224
卷: 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
所属项目编号: 0430076N ; AR40615 ; 30330160 ; 30370379 ; 2004CB720005
项目资助者: 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
WOS记录号: WOS:000260072600022
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/51360
Appears in Collections:基础医学院_生物物理学系_期刊论文

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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

Recommended Citation:
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.
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