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1uuo
From Proteopedia
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Revision as of 14:07, 30 October 2007
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RAT DIHYDROOROTATE DEHYDROGENASE (DHOD)IN COMPLEX WITH BREQUINAR
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
1UUO is a [Single protein] structure of sequence from [Rattus rattus] with NI, NA, BRF, FMN and ORO 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 16:11:54 2007
Categories: Dihydroorotate dehydrogenase | Rattus rattus | Single protein | Antal, T. | Hansen, M. | Johansson, E. | Larsen, S. | Loffler, M. | Nours, J.Le. | Ullrich, A. | BRF | FMN | NA | NI | ORO | Atovaquone | Brequinar | Nucleotide metabolism | Oxidoreductase
