Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-Å resolution
Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-Å resolution
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DOI：
10.1074/jbc.m107804200
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发表时间：
2001-11-30
影响因子：
4.8
通讯作者：
Curmi, PMG
中科院分区：
文献类型：
--
作者：
Harrop, SJ;DeMaere, MZ;Curmi, PMG
CLIC1 （NCC27）是一种高度保守的氯离子通道，存在于可溶性和整体膜形式中。纯化的CLIC1可以整合到合成的脂质双分子层中，形成与体内观察到的氯离子通道相似的性质。在1.4埃分辨率下测定了CLIC1的可溶性结构。该蛋白为单体，结构上与谷胱甘肽s -转移酶超家族同源，具有类似于谷胱甘肽的氧化还原活性位点。CLIC1与谷胱甘肽复合物的结构表明，谷胱甘肽占据了氧化还原活性位点，该位点毗邻一个由碱性残基排列的开放的细长槽。将CLIC1整合到膜中可能需要一个主要的结构重排，可能是n结构域（残基1-90），假设的跨膜螺旋是由氧化还原活性位点附近的残基产生的。该结构表明CLIC1可能是由氧化还原依赖的进程控制的。
CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exists in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to those observed in vivo. The structure of the soluble form of CLIC1 has been determined at 1.4-Angstrom resolution. The protein is monomeric and structurally homologous to the glutathione S-transferase superfamily, and it has a redox-active site resembling glutaredoxin. The structure of the complex of CLIC1 with glutathione shows that glutathione occupies the redox-active site, which is adjacent to an open, elongated slot lined by basic residues. Integration of CLIC1 into the membrane is likely to require a major structural rearrangement, probably of the N-domain (residues 1-90), with the putative transmembrane helix arising from residues in the vicinity of the redox-active site. The structure indicates that CLIC1 is likely to be controlled by redox-dependent processes.