Structural plasticity in MS channels

被引：7

作者：

Martinac, B ^{[1
]}

机构：

[1] Univ Queensland, Sch Biomed Sci, Brisbane, Qld 4072, Australia

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2005年 / 12卷 / 02期

关键词：

D O I：

10.1038/nsmb0205-104

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Gating of the mechanosensitive channel MscS involves cooperative action of glycine and alanine residues along the pore-lining transmembrane helix. Opening of the channel is facilitated by an iris-like rotation and tilt of the pore-lining helices. Site-directed mutagenesis indicates that substantial structural plasticity can be tolerated by MscS without impairing its function.

引用

页码：104 / 105

页数：2

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