Binding of transition metals to S100 proteins

被引:0
作者
Benjamin A. Gilston
Eric P. Skaar
Walter J. Chazin
机构
[1] Vanderbilt University,Departments of Biochemistry and Chemistry, and Center for Structural Biology
[2] Vanderbilt University Medical Center,Department of Pathology, Microbiology and Immunology
来源
Science China Life Sciences | 2016年 / 59卷
关键词
S100 Proteins; Zinc; Manganese; Copper;
D O I
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中图分类号
学科分类号
摘要
The S100 proteins are a unique class of EF-hand Ca2+ binding proteins distributed in a cell-specific, tissue-specific, and cell cycle-specific manner in humans and other vertebrates. These proteins are distinguished by their distinctive homodimeric structure, both intracellular and extracellular functions, and the ability to bind transition metals at the dimer interface. Here we summarize current knowledge of S100 protein binding of Zn2+, Cu2+ and Mn2+ ions, focusing on binding affinities, conformational changes that arise from metal binding, and the roles of transition metal binding in S100 protein function.
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页码:792 / 801
页数:9
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