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处于关闭状态的钾通道KirBac1.1的晶体结构。

Crystal structure of the potassium channel KirBac1.1 in the closed state.

作者信息

Kuo Anling, Gulbis Jacqueline M, Antcliff Jennifer F, Rahman Tahmina, Lowe Edward D, Zimmer Jochen, Cuthbertson Jonathan, Ashcroft Frances M, Ezaki Takayuki, Doyle Declan A

机构信息

University of Oxford, Department of Biochemistry, Laboratory of Molecular Biophysics, South Parks Road, Oxford OX1 3QU, UK.

出版信息

Science. 2003 Jun 20;300(5627):1922-6. doi: 10.1126/science.1085028. Epub 2003 May 8.

DOI:10.1126/science.1085028
PMID:12738871
Abstract

The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in gating. On the basis of structural evidence presented here, we suggest that gating involves coupling between the intracellular and membrane domains. This further suggests that initiation of gating by membrane or intracellular signals represents different entry points to a common mechanistic pathway.

摘要

KirBac1.1通道属于钾通道内向整流器家族。在此,我们报告了处于关闭状态的整个原核Kir通道组件的结构,其分辨率提高到了3.65埃。我们确定了主要的激活门控及参与门控的结构元件。基于此处提供的结构证据,我们认为门控涉及细胞内结构域与膜结构域之间的偶联。这进一步表明,由膜信号或细胞内信号引发的门控代表了通向共同机制途径的不同切入点。

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