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

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Braun, W, Vasák, M, Robbins, A H, Stout, C D, Wagner, G, Kägi, J H, Wüthrich, K·1992·Proceedings of the National Academy of Sciences

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., 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.

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Metadata

Authors
Braun, W., Vasák, M., Robbins, A. H., Stout, C. D., Wagner, G., Kägi, J. H., & Wüthrich, K.
Venue
Proceedings of the National Academy of Sciences
Published
1992-11
Volume
89
Issue
21
Pages
10124-10128
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1980139350
Cited by
231
References
0
FWCI
4.31
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2. https://app.cochat.ai/papers/10.1073/pnas.89.21.10124
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Braun, W., Vasák, M., Robbins, A. H., Stout, C. D., Wagner, G., Kägi, J. H., & Wüthrich, K. (1992). Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.21.10124

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