A place for thioether chemistry in cellular copper ion recognition and trafficking

被引：197

作者：

Davis, Anna V.

O'Halloran, Thomas V. ^{[1
]}

机构：

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

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

来源：

NATURE CHEMICAL BIOLOGY | 2008年 / 4卷 / 03期

关键词：

D O I：

10.1038/nchembio0308-148

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：

Over the last decade, cysteine thiolate ligands have been shown to be critical to the Cu(I) (cuprous) binding chemistry of many cytosolic metallochaperone and metalloregulatory proteins involved in copper physiology. More recently, the thioether group of methionine has begun to emerge as an important Cu(I) ligand for trafficking proteins in more oxidizing cellular environments.

引用

页码：148 / 151

页数：4

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