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4mt2

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(New page: 200px<br /><applet load="4mt2" size="450" color="white" frame="true" align="right" spinBox="true" caption="4mt2, resolution 2.0&Aring;" /> '''COMPARISON OF THE NMR...)
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[[Image:4mt2.gif|left|200px]]<br /><applet load="4mt2" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:4mt2.gif|left|200px]]<br /><applet load="4mt2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="4mt2, resolution 2.0&Aring;" />
caption="4mt2, resolution 2.0&Aring;" />
'''COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL STRUCTURE OF RAT METALLOTHIONEIN-2'''<br />
'''COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL STRUCTURE OF RAT METALLOTHIONEIN-2'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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4MT2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with CD, ZN, NA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4MT2 OCA].
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4MT2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MT2 OCA].
==Reference==
==Reference==
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[[Category: Rattus rattus]]
[[Category: Rattus rattus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Robbins, A.H.]]
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[[Category: Robbins, A H.]]
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[[Category: Stout, C.D.]]
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[[Category: Stout, C D.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: CD]]
[[Category: CD]]
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[[Category: metallothionein]]
[[Category: metallothionein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:43:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:54 2008''

Revision as of 17:13, 21 February 2008


4mt2, resolution 2.0Å

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

Overview

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.

About this Structure

4MT2 is a Single protein structure of sequence from Rattus rattus with , , and as ligands. 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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