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| [[Image:4mt2.gif|left|200px]] | | {{Seed}} |
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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'''
| | ===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. & 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_1438200}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 1438200 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_1438200}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Stout, C D.]] | | [[Category: Stout, C D.]] |
| [[Category: Metallothionein]] | | [[Category: Metallothionein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:27:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:44:44 2008'' |
