大鼠金属硫蛋白-2的核磁共振溶液结构与X射线晶体结构的比较。
Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.
作者信息
Braun W, Vasák M, Robbins A H, Stout C D, Wagner G, Kägi J H, Wüthrich K
机构信息
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, Zürich, Switzerland.
出版信息
Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10124-8. doi: 10.1073/pnas.89.21.10124.
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., Wörgötter, E., Braun, W., Wagner, G., Vasák, M., Kägi, J. H. R. & Wüthrich, K. (1988) J. Mol. Biol. 203, 251-268] 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.
金属硫蛋白是一类富含半胱氨酸的小蛋白，能够结合重金属离子，如Zn2+和Cd2+。它们是高等生物中普遍存在的组织成分，初步认为其具有针对有毒金属离子的非特异性保护功能以及在锌调控的基本细胞过程中发挥高度特异性作用。本文对大鼠金属硫蛋白-2的核磁共振溶液结构[舒尔茨，P.，沃格特，E.，布劳恩，W.，瓦格纳，G.，瓦萨克，M.，凯吉，J. H. R. & 伍特里希，K.（1988年）《分子生物学杂志》203卷，251 - 268页]和最近的X射线晶体结构[罗宾斯，A. H.，麦克里，D. E.，威廉姆森，M.，科利特，S. A.，熊，N. H.，富雷，W. F.，王，B. C. & 斯托特，C. D.（1991年）《分子生物学杂志》221卷，1269 - 1293页]进行了详细比较，结果表明晶体中和溶液中的金属硫蛋白结构具有相同的分子结构。现在，这两种技术获得的结构为讨论这类金属蛋白的结构 - 功能相关性提供了可靠的基础。
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