1r5y
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(New page: 200px<br /><applet load="1r5y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r5y, resolution 1.20Å" /> '''Crystal Structure of...)
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Revision as of 23:10, 20 November 2007
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Crystal Structure of TGT in complex with 2,6-Diamino-3H-Quinazolin-4-one Crystallized at PH 5.5
Overview
The enzyme tRNA-guanine transglycosylase (TGT) is involved in the, pathogenicity of Shigellae. As the crystal structure of this protein is, known, it is a putative target for the structure-based design of, inhibitors. Here we report a crystallographic study of several new ligands, exhibiting a 2,6-diamino-3H-quinazolin-4-one scaffold, which has been, shown recently to be a promising template for TGT-inhibitors. Crystal, structure analysis of these complexes has revealed an unexpected movement, of the side-chain of Asp102. A detailed analysis of the water network, disrupted by this rotation has lead to the derivation of a new composite, pharmacophore. A virtual screening has been performed based on this, pharmacophore hypothesis and several new inhibitors of micromolar binding, affinity with new skeletons have been discovered.
About this Structure
1R5Y is a Single protein structure of sequence from Zymomonas mobilis with ZN and DQU as ligands. Active as Queuine tRNA-ribosyltransferase, with EC number 2.4.2.29 Full crystallographic information is available from OCA.
Reference
Crystallographic study of inhibitors of tRNA-guanine transglycosylase suggests a new structure-based pharmacophore for virtual screening., Brenk R, Meyer EA, Reuter K, Stubbs MT, Garcia GA, Diederich F, Klebe G, J Mol Biol. 2004 Apr 16;338(1):55-75. PMID:15050823
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