Advances in the structure and chemistry of metallothioneins

被引：225

作者：

Romero-Isart, N ^{[1
]}

Vasák, M ^{[1
]}

机构：

[1] Univ Zurich, Inst Biochem, CH-8057 Zurich, Switzerland

来源：

JOURNAL OF INORGANIC BIOCHEMISTRY | 2002年 / 88卷 / 3-4期

关键词：

metallothionein; protein structure; metal-thiolate clusters; structure dynamics; thiol reactivity;

D O I：

10.1016/S0162-0134(01)00347-6

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：

A low molecular weight (6-7 kDa) class of metalloproteins, designated as metallothioneins (MTs), exhibit repeated sequence motifs of either CxC or CxxC through which mono or divalent d(10) metal ions are bound in polymetallic-thiolate clusters. The preservation of metal-thiolate clusters in an increasing number of three-dimensional structures of these proteins signifies the importance of this structural motif. This review focuses on the recent developments regarding the versatile and striking chemical reactivity of MTs as well as on the existence of conformational/configurational dynamics within their structure. Both properties and their interplay are likely to be essential for the still elusive biological function of these proteins. (C) 2002 Elsevier Science Inc. All rights reserved.

引用

页码：388 / 396

页数：9

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