1uum
From Proteopedia
(New page: 200px<br /> <applet load="1uum" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uum, resolution 2.3Å" /> '''RAT DIHYDROOROTATE D...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1UUM 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 BOG, FMN, ORO and AFI as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.11 1.3.99.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UUM OCA]]. | + | 1UUM 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 BOG, FMN, ORO and AFI as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Dihydroorotate_dehydrogenase Dihydroorotate dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.11 1.3.99.11]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UUM OCA]]. |
==Reference== | ==Reference== | ||
Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain., Hansen M, Le Nours J, Johansson E, Antal T, Ullrich A, Loffler M, Larsen S, Protein Sci. 2004 Apr;13(4):1031-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15044733 15044733] | Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain., Hansen M, Le Nours J, Johansson E, Antal T, Ullrich A, Loffler M, Larsen S, Protein Sci. 2004 Apr;13(4):1031-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15044733 15044733] | ||
| + | [[Category: Dihydroorotate dehydrogenase]] | ||
[[Category: Rattus rattus]] | [[Category: Rattus rattus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:25:05 2007'' |
Revision as of 09:20, 30 October 2007
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RAT DIHYDROOROTATE DEHYDROGENASE (DHOD)IN COMPLEX WITH ATOVAQUONE
Overview
The flavin enzyme dihydroorotate dehydrogenase (DHOD; EC 1.3.99.11), catalyzes the oxidation of dihydroorotate to orotate, the fourth step in, the de novo pyrimidine biosynthesis of UMP. The enzyme is a promising, target for drug design in different biological and clinical applications, for cancer and arthritis. The first crystal structure of the class 2, dihydroorotate dehydrogenase from rat has been determined in complex with, its two inhibitors brequinar and atovaquone. These inhibitors have shown, promising results as anti-proliferative, immunosuppressive, and, antiparasitic agents. A unique feature of the class 2 DHODs is their, N-terminal extension, which folds into a separate domain comprising two, alpha-helices. This domain serves as the binding site for the two, inhibitors and ... [(full description)]
About this Structure
1UUM is a [Single protein] structure of sequence from [Rattus rattus] with BOG, FMN, ORO and AFI as [ligands]. Active as [Dihydroorotate dehydrogenase], with EC number [1.3.99.11]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain., Hansen M, Le Nours J, Johansson E, Antal T, Ullrich A, Loffler M, Larsen S, Protein Sci. 2004 Apr;13(4):1031-42. PMID:15044733
Page seeded by OCA on Tue Oct 30 11:25:05 2007
Categories: Dihydroorotate dehydrogenase | Rattus rattus | Single protein | Antal, T. | Hansen, M. | Johansson, E. | Larsen, S. | Loffler, M. | Nours, J.Le. | Ullrich, A. | AFI | BOG | FMN | ORO | Atovaquone | Brequinar | Fad | Flavoprotein | Nucleotide metabolism | Oxidoreductase | Pyrimidine biosynthesis | Transit peptide
