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1wnt

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(New page: 200px<br /> <applet load="1wnt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wnt, resolution 2.30&Aring;" /> '''Strucutre of the te...)
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Revision as of 17:46, 12 November 2007

Image:1wnt.gif

1wnt, resolution 2.30Å

Drag the structure with the mouse to rotate

Strucutre of the tetrameric form of Human L-Xylulose Reductase

Overview

L-Xylulose reductase (XR) is a member of the short-chain, dehydrogenase/reductase (SDR) superfamily. In this study we report the, structure of the biological tetramer of human XR in complex with NADP(+), and a competitive inhibitor solved at 2.3 A resolution. A single subunit, of human XR is formed by a centrally positioned, seven-stranded, parallel, beta-sheet surrounded on either side by two arrays of three alpha-helices., Two helices located away from the main body of the protein form the, variable substrate-binding cleft, while the dinucleotide coenzyme-binding, motif is formed by a classical Rossmann fold. The tetrameric structure of, XR, which is held together via salt bridges formed by the guanidino group, of Arg203 from one monomer and the carboxylate group of the C-terminal, residue Cys244 from the neighboring monomer, explains the ability of human, XR to prevent the cold inactivation seen in the rodent forms of the, enzyme. The orientations of Arg203 and Cys244 are maintained by a network, of hydrogen bonds and main-chain interactions of Gln137, Glu238, Phe241, and Trp242. These interactions are similar to those defining the, quaternary structure of the closely related carbonyl reductase from mouse, lung. Molecular modeling and site-directed mutagenesis identified the, active site residues His146 and Trp191 as forming essential contacts with, inhibitors of XR. These results could provide a structural basis in the, design of potent and specific inhibitors for human XR.

About this Structure

1WNT is a Single protein structure of sequence from Homo sapiens with NAP as ligand. Active as L-xylulose reductase, with EC number 1.1.1.10 Full crystallographic information is available from OCA.

Reference

Structure of the tetrameric form of human L-Xylulose reductase: probing the inhibitor-binding site with molecular modeling and site-directed mutagenesis., El-Kabbani O, Carbone V, Darmanin C, Ishikura S, Hara A, Proteins. 2005 Aug 15;60(3):424-32. PMID:15906319

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