Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2

W. Braun, M. Vasak, A. H. Robbins, C. D. Stout, G. Wagner, J. H.R. Kagi, K. Wuthrich

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Abstract

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. and Wuthrich, 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. and 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.

Original languageEnglish (US)
Pages (from-to)10124-10128
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number21
DOIs
StatePublished - Nov 17 1992

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