Structure and chemistry of the copper chaperone proteins

被引：173

作者：

Rosenzweig, AC

O'Halloran, TV

机构：

[1] Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA

[2] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2000年 / 4卷 / 02期

关键词：

D O I：

10.1016/S1367-5931(99)00066-6

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：

Major advances have been made in the past year towards an understanding of the structure and chemistry of copper chaperone proteins. Three-dimensional structures of Atx1, CopZ, yCCS, and hCCSdll were determined, and reveal a remarkable structural similarity between chaperones and target proteins. In addition, biochemical studies of CCS suggested that chaperones are required in vivo because intracellular copper concentrations are extremely low and also indicated that copper transfer occurs via a direct protein-protein interaction.

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收藏

页码：140 / 147

页数：8

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