3epw

Crystal structure of Trypanosoma vivax nucleoside hydrolase in complex with the inhibitor (2R,3R,4S)-1-[(4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidin-3,4-diol

spinqualitylabelsall models 3epw, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3epw is a 2 chain structure with sequence from Duttonella vivax. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, JMQ, MG Related: 2ff2, 1hoz, 1hp0, 1kic, 3b9g, 3epx Activity: Purine nucleosidase, with EC number 3.2.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Diseases caused by parasitic protozoa remain a major health problem, mainly due to old toxic drugs and rising drug resistance. Nucleoside hydrolases are key enzymes of the purine salvage pathway of parasites from the Trypanosomatidae family and are considered as possible drug targets. N-Arylmethyl substituted iminoribitols have been developed as selective nanomolar affinity inhibitors against the purine-specific nucleoside hydrolase of Trypanosoma vivax. The current paper describes the crystal structures of the T. vivax nucleoside hydrolase in complex with two of these inhibitors, to 1.3 and 1.85 A resolution. These high resolution structures provide an accurate picture of the mode of binding of these inhibitors and their mechanism of transition-state mimicry, and are valuable tools to guide further inhibitor design. Comparison of the current structures with previously solved structures of the enzyme in complex with ground-state and transition-state-analogue inhibitors also allows for the elucidation of a detailed molecular mechanism of active-site loop opening/closing. These loop movements can be coupled to the complex kinetic mechanism of the T. vivax nucleoside hydrolase. Crystal structures of T. vivax nucleoside hydrolase in complex with new potent and specific inhibitors.,Versees W, Goeminne A, Berg M, Vandemeulebroucke A, Haemers A, Augustyns K, Steyaert J Biochim Biophys Acta. 2009 Jun;1794(6):953-60. Epub 2009 Mar 10. PMID:19281874 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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