COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL-STRUCTURE OF RAT METALLOTHIONEIN-2
COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL-STRUCTURE OF RAT METALLOTHIONEIN-2
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DOI：
10.1073/pnas.89.21.10124
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发表时间：
1992-11-01
影响因子：
11.1
通讯作者：
WUTHRICH, K
中科院分区：
文献类型：
--
作者：
BRAUN, W;VASAK, M;WUTHRICH, K
金属硫蛋白是一种富含半胱氨酸的小分子蛋白质，能够结合重金属离子，如Zn 2+和Cd 2+。它们是高等生物中普遍存在的组织成分，暂时被认为具有针对有毒金属离子的非特异性保护功能和在基本锌调节细胞过程中的高度特异性作用。本文详细比较了NMR溶液结构[Schultze，P.，Worgotter，E.，Braun，W.，瓦格纳，G.，Vasak，M.，Kagi，J. H. R. & Wuthrich，K.等人（1988）J. Mol. 203，251-2681和最近的X射线晶体结构[Robbins，A. H、McRee，D. E、威廉姆森，M.，Collett，S.一、克塞登，N. H、Furey，W. F.、Wang，B. C. & Stout，C. D.等人（1991）J. Mol. Biol.221，1269-1293]显示晶体和溶液中的金属硫蛋白结构具有相同的分子结构。这两种技术获得的结构，现在提出了一个可靠的基础上讨论这类金属蛋白的结构-功能相关性。
Metallothioneins are small cysteine-rich proteins capable of binding heavy metal ions such as Zn2+ and Cd2+. They are ubiquitous tissue components in higher organisms, which tentatively have been attributed both unspecific protective functions against toxic metal ions and highly specific roles in fundamental zinc-regulated cellular processes. In this paper a detailed comparison of the NMR solution structure [Schultze, P., Worgotter, E., Braun, W., Wagner, G., Vasak, M., Kagi, J. H. R. & Wuthrich, K. (1988) J. Mol. Biol. 203, 251-2681 and a recent x-ray crystal structure [Robbins, A. H., McRee, D. E., Williamson, M., Collett, S. A., Xoung, N. H., Furey, W. F., Wang, B. C. & Stout, C. D. (1991) J. Mol. Biol. 221, 1269-1293] of rat metallothionein-2 shows that the metallothionein structures in crystals and in solution have identical molecular architectures. The structures obtained with both techniques now present a reliable basis for discussions on structure-function correlations in this class of metalloproteins.