View source for 2p4d


==Structure-assisted discovery of Variola major H1 phosphatase inhibitors==
<StructureSection load='2p4d' size='340' side='right'caption='[[2p4d]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2p4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Varv Varv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P4D FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p4d OCA], [https://pdbe.org/2p4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p4d RCSB], [https://www.ebi.ac.uk/pdbsum/2p4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p4d ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/DUSP_VAR67 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p4/2p4d_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2p4d ConSurf].
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== 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<ref>PMID:17505108</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[MAP kinase phosphatase|MAP kinase phosphatase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Varv]]
[[Category: Phan, J]]
[[Category: Tropea, J E]]
[[Category: Waugh, D S]]
[[Category: Drug design]]
[[Category: Dual specificity phosphatase]]
[[Category: Enzyme]]
[[Category: Hydrolase]]
[[Category: Small pox]]