期刊
JOURNAL OF GENERAL PHYSIOLOGY
卷 122, 期 6, 页码 741-748出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1085/jgp.200308927
关键词
Shaker K channel; voltage gated; disulfide; S4 movement; helical screw
类别
资金
- NINDS NIH HHS [R01 NS043259, NS043259] Funding Source: Medline
The X-ray crystallographic structure of KvAP, a voltage-gated bacterial K channel, was recently published. However, the position and the molecular movement of the voltage sensor, S4, are still controversial. For example, in the crystallographic structure, S4 is located far away (>30 Angstrom) from the pore domain, whereas electrostatic experiments have suggested that S4 is located close (<8 Angstrom) to the pore domain in open channels. To test the proposed location and motion of S4 relative to the pore domain, we induced disulphide bonds between pairs of introduced cysteines: one in S4 and one in the pore domain. Several residues in S4 formed a state-dependent disulphide bond with a residue in the pore domain. Our data suggest that S4 is located close to the pore domain in a neighboring subunit. Our data also place constraints on possible models for S4 movement and are not compatible with a recently proposed KvAP model.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据