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4o6h

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o6h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o6h RCSB], [http://www.ebi.ac.uk/pdbsum/4o6h PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o6h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o6h RCSB], [http://www.ebi.ac.uk/pdbsum/4o6h PDBsum]</span></td></tr>
<table>
<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The X-ray crystal structure of the Lymphocytic choriomeningitis virus nucleoprotein C-terminal immunosuppressive domain (LCMV NPDelta340) was determined to 2.0 A resolution. The structure indicates that LCMV NPDelta340, like the other structurally characterized arenaviral nucleoproteins, adopts the fold of an exonuclease. This structure provides a crucial three-dimensional template for functional exploration of the replication and immunosuppression of this prototypic arenavirus.
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Structure of the LCMV nucleoprotein provides a template for understanding arenavirus replication and immunosuppression.,West BR, Hastie KM, Saphire EO Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1764-9. doi:, 10.1107/S1399004714007883. Epub 2014 May 30. PMID:24914986<ref>PMID:24914986</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 06:26, 2 July 2014

2.8A crystal structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-terminal Domain

4o6h, resolution 2.80Å

Drag the structure with the mouse to rotate

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