1uum

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Revision as of 15:47, 29 October 2007

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spinqualitylabelsall models 1uum, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 [[1]], with EC number [1.3.99.11]. 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

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