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学科主题: 基础医学
题名:
Structural and functional analysis of natrin, a venom protein that targets various ion channels
作者: Wang, Feng; Li, He; Liu, Ming-na; Song, Hui; Han, Hong-mei; Wang, Qiong-ling; Yin, Chang-chen; Zhou, Yuan-cong; Qi, Zhi; Shu, Yu-yan; Lin, Zheng-jiong; Jiang, Tao
关键词: CRISP ; natrin ; crystal structure ; blocker ; ion channel
刊名: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
发表日期: 2006-12-15
DOI: 10.1016/j.bbrc.2006.10.067
卷: 351, 期:2, 页:443-448
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemistry & Molecular Biology ; Biophysics
研究领域[WOS]: Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]: RICH SECRETORY PROTEIN ; CRYSTAL-STRUCTURE ; CRISP FAMILY ; POTASSIUM CHANNELS ; K+ CHANNEL ; CYSTEINE-RICH-SECRETORY-PROTEIN-4 CRISP4 ; LIZARD VENOM ; SNAKE-VENOM ; TOXIN ; HELOTHERMINE
英文摘要:

Cysteine-rich secretory proteins (CRISPs) are secreted single-chain proteins found in different sources. Natrin is a member of the CRISP family purified from the snake venom of Naja naja atra, which has been reported as a BKca channel blocker. In our study, crystals of natrin were obtained in two different crystal forms and the structure of one of them was solved at a resolution of 1.68 angstrom. Our electrophysiological experiments indicated that natrin can block the ion channel currents of the voltage-gated potassium channel Kv1.3. Docking analyses of the interaction between natrin and Kv1.3 revealed a novel interaction pattern different from the two previously reported K+ channel inhibition models termed "functional dyad" and "basic ring". These findings offered new insights into the function of natrin and how the specific interactions between CRISPs and different ion channels can be achieved. (c) 2006 Elsevier Inc. All rights reserved.

语种: 英语
WOS记录号: WOS:000242119200021
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/65499
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.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
2.Chinese Acad Sci, Inst Biophys, State Key Lab Brain & Cognit Sci, Beijing 100101, Peoples R China
3.Guangxi Med Univ, Snake Venom Res Inst, Nanning 530021, Guangxi, Peoples R China
4.Peking Univ, Hlth Sci Ctr, Dept Biophys, Beijing 100083, Peoples R China
5.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Key Lab Proteom, Shanghai 200031, Peoples R China
6.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China

Recommended Citation:
Wang, Feng,Li, He,Liu, Ming-na,et al. Structural and functional analysis of natrin, a venom protein that targets various ion channels[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2006,351(2):443-448.
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