From glutathione transferase to pore in a CLIC

被引:77
作者
Cromer, BA
Morton, CJ
Board, PG
Parker, MW
机构
[1] St Vincents Inst Med Res, Biota Struct Biol Lab, Fitzroy, Vic 3065, Australia
[2] Australian Natl Univ, John Curtin Sch Med Res, Canberra, ACT 2601, Australia
来源
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2002年 / 31卷 / 05期
基金
澳大利亚研究理事会; 英国医学研究理事会;
关键词
chloride channels; crystal structures; CLICs; glutathione transferases; pore-forming toxins;
D O I
10.1007/s00249-002-0219-1
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Many plasma membrane chloride channels have been cloned and characterized in great detail. In contrast, very little is known about intracellular chloride channels. Members of a novel class of such channels, called the CLICs (chloride intracellular channels), have been identified over the last few years. A striking feature of the CLIC family of ion channels is that they can exist in a water-soluble state as well as a membrane-bound state. A major step forward in understanding the functioning of these channels has been the recent crystal structure determination of one family member, CLICI. The structure confirms that CLICs are members of the glutathione S-transferase superfamily and provides clues as to how CLICs can insert into membranes to form chloride channels.
引用
收藏
页码:356 / 364
页数:9
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