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

被引：624

作者：

Kuo, AL

Gulbis, JM

Antcliff, JF

Rahman, T

Lowe, ED

Zimmer, J

Cuthbertson, J

Ashcroft, FM

Ezaki, T

Doyle, DA ^{[1
]}

机构：

[1] Univ Oxford, Dept Biochem, Lab Mol Biophys, Oxford OX1 3QU, England

[2] Walter & Eliza Hall Inst Med Res, Struct Biol Div, Parkville, Vic 3050, Australia

[3] Univ Oxford, Physiol Lab, Oxford OX1 3PT, England

[4] Gifu Univ, Grad Sch Med Regenerat & Adv Med Sci, Dept Microbiol & Bioinformat, Gifu 5008705, Japan

来源：

SCIENCE | 2003年 / 300卷 / 5627期

关键词：

D O I：

10.1126/science.1085028

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：1922 / 1926

页数：5

共 27 条

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