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

@article{Braun1992ComparisonOT,
  title={Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.},
  author={Werner Braun and Milan Va{\vs}{\'a}k and Arthur H. Robbins and Charles David Stout and Gerhard Wagner and Jeremias H. R. K{\"a}gi and Kurt W{\"u}thrich},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1992},
  volume={89 21},
  pages={10124-8}
}
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. & W… CONTINUE READING

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J . Mol . Biol . 221 , 533 - 555

  • A. H. Robbins, C. D. Stout
  • Proc . Natd . Acad . Sci . USA
  • 1991

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