Copper delivery by metallochaperone proteins

被引：234

作者：

Rosenzweig, AC ^{[1
]}

机构：

[1] Northwestern Univ, Dept Biochem, Evanston, IL 60208 USA

[2] Northwestern Univ, Dept Mol Biol, Evanston, IL 60208 USA

[3] Northwestern Univ, Dept Cell Biol, Evanston, IL 60208 USA

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

来源：

ACCOUNTS OF CHEMICAL RESEARCH | 2001年 / 34卷 / 02期

关键词：

D O I：

10.1021/ar000012p

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Copper is an essential element in all living organisms, serving as a cofactor for many important proteins and enzymes. Metallochaperone proteins deliver copper ions to specific physiological partners by direct protein-protein interactions. The Atx1-like chaperones transfer copper to intracellular copper transporters, and the CCS chaperones shuttle copper to copper, zinc superoxide dismutase. Crystallographic studies of these two copper chaperone families have provided insights into metal binding and target recognition by metallochaperones and have led to detailed molecular models for the copper transfer mechanism.

引用

页码：119 / 128

页数：10

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