4mt2

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{{STRUCTURE_4mt2| PDB=4mt2 | SCENE= }}
{{STRUCTURE_4mt2| PDB=4mt2 | SCENE= }}
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'''COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL STRUCTURE OF RAT METALLOTHIONEIN-2'''
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===COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL STRUCTURE OF RAT METALLOTHIONEIN-2===
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==Overview==
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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. &amp; 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. &amp; 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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{{ABSTRACT_PUBMED_1438200}}
==About this Structure==
==About this Structure==
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[[Category: Stout, C D.]]
[[Category: Stout, C D.]]
[[Category: Metallothionein]]
[[Category: Metallothionein]]
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Revision as of 10:44, 3 July 2008

Template:STRUCTURE 4mt2

COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL STRUCTURE OF RAT METALLOTHIONEIN-2

Template:ABSTRACT PUBMED 1438200

About this Structure

4MT2 is a Single protein structure of sequence from Rattus rattus. Full crystallographic information is available from OCA.

Reference

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

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