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From Proteopedia
High Resolution Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1
Structural highlights
Function[DUSP_VACCW] 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.[1] [2] [3] [4] [5] 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 PubMedThe Vaccinia virus H1 gene product, VH1, is a dual specificity phosphatase that down-regulates the cellular antiviral response by dephosphorylating STAT1. The crystal structure of VH1, determined at 1.32 A resolution, reveals a novel dimeric quaternary structure, which exposes two active sites spaced approximately 39 A away from each other. VH1 forms a stable dimer via an extensive domain swap of the N-terminal helix (residues 1-20). In vitro, VH1 can dephosphorylate activated STAT1, in a reaction that is competed by the nuclear transport adapter importin alpha5. Interestingly, VH1 is inactive with respect to STAT1 bound to DNA, suggesting that the viral phosphatase acts predominantly on the cytoplasmic pool of activated STAT1. We propose that the dimeric quaternary structure of VH1 is essential for specific recognition of activated STAT1, which prevents its nuclear translocation, thus blocking interferon-gamma signal transduction and antiviral response. Dimeric quaternary structure of the prototypical dual specificity phosphatase VH1.,Koksal AC, Nardozzi JD, Cingolani G J Biol Chem. 2009 Apr 10;284(15):10129-37. Epub 2009 Feb 10. PMID:19211553[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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