Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Phan J, Tropea JE, Waugh DS. Structure-assisted discovery of Variola major H1 phosphatase inhibitors. Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):698-704. Epub 2007, May 15. PMID:17505108 doi:10.1107/S0907444907014904
