Functional properties of the human copper-transporting ATPase ATP7B (the Wilson's disease protein) and regulation by metallochaperone Atox1

被引：28

作者：

Lutsenko, S ^{[1
]}

Tsivkovskii, R ^{[1
]}

Walker, JM ^{[1
]}

机构：

[1] Oregon Hlth Sci Univ, Dept Biochem & Mol Biol, Portland, OR 97239 USA

来源：

NA,K-ATPASE AND RELATED CATION PUMPS: STRUCTURE, FUNCTION, AND REGULATORY MECHANISMS | 2003年 / 986卷

关键词：

ATP7B; copper; Wilson's disease; metallochaperone; Atox1; regulation;

D O I：

10.1111/j.1749-6632.2003.tb07161.x

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：

Wilson's disease protein (WNDP) is a copper-transporting P-1-type ATPase which plays a key role in normal distribution of copper in a number of tissues, particularly in the liver and the brain. Copper has numerous effects on WNDP, altering its structure, activity, and intracellular localization. To better understand the function of this copper-transporting ATPase and its regulation by copper, we have recently developed the functional expression systems for WNDP and for Atox1, a cytosolic protein that serves as an intracellular donor of copper for WNDP. Here we summarize the results of our experiments on characterization of the enzymatic properties of WNDP and the effects of Atox1 on the WNDP activity.

引用

页码：204 / 211

页数：8

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