Structural highlights
Function
[MT2_RAT] Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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, 251-268] 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.
Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.,Braun W, Vasak M, Robbins AH, Stout CD, Wagner G, Kagi JH, Wuthrich K Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10124-8. PMID:1438200[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Braun W, Vasak M, Robbins AH, Stout CD, Wagner G, Kagi JH, Wuthrich K. Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2. Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10124-8. PMID:1438200
