Romero-Isart Núria, Vasák Milan
Institute of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
J Inorg Biochem. 2002 Feb;88(3-4):388-96. doi: 10.1016/s0162-0134(01)00347-6.
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.
一类低分子量（6 - 7千道尔顿）的金属蛋白，被称为金属硫蛋白（MTs），具有CxC或CxxC的重复序列基序，通过这些基序，单价或二价d(10)金属离子在多金属硫醇盐簇中结合。这些蛋白质越来越多的三维结构中金属硫醇盐簇的保留表明了这种结构基序的重要性。本综述聚焦于金属硫蛋白多样且显著的化学反应性的最新进展，以及其结构中构象/构型动力学的存在。这两种特性及其相互作用可能对于这些蛋白质仍难以捉摸的生物学功能至关重要。
