2p4d

Structure-assisted discovery of Variola major H1 phosphatase inhibitors

spinqualitylabelsall models 2p4d, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2p4d is a 1 chain structure with sequence from Varv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DUSP_VAR67] Serine/Tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the A17 protein (By similarity). 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 Variola major virus, the causative agent of smallpox, encodes the dual-specificity H1 phosphatase. Because this enzyme is essential for the production of mature virus particles, it is an attractive molecular target for the development of therapeutic countermeasures for this potential agent of bioterrorism. As a first step in this direction, the crystal structure of H1 phosphatase has been determined at a resolution of 1.8 A. In silico screening methods have led to the identification of several small molecules that inhibit Variola H1 phosphatase with IC(50) values in the low micromolar range. These molecules provide novel leads for future drug development. Structure-assisted discovery of Variola major H1 phosphatase inhibitors.,Phan J, Tropea JE, Waugh DS Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):698-704. Epub 2007, May 15. PMID:17505108 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also MAP kinase phosphatase

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