View source for 4blg


==Crystal structure of MHV-68 Latency-associated nuclear antigen (LANA) C-terminal DNA binding domain==
<StructureSection load='4blg' size='340' side='right'caption='[[4blg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4blg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Murid_gammaherpesvirus_4 Murid gammaherpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BLG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4blg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4blg OCA], [https://pdbe.org/4blg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4blg RCSB], [https://www.ebi.ac.uk/pdbsum/4blg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4blg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O41974_MHV68 O41974_MHV68] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Latency-associated nuclear antigen (LANA) mediates gamma2-herpesvirus genome persistence and regulates transcription. We describe the crystal structure of the murine gammaherpesvirus-68 LANA C-terminal domain at 2.2 A resolution. The structure reveals an alpha-beta fold that assembles as a dimer, reminiscent of Epstein-Barr virus EBNA1. A predicted DNA binding surface is present and opposite this interface is a positive electrostatic patch. Targeted DNA recognition substitutions eliminated DNA binding, while certain charged patch mutations reduced bromodomain protein, BRD4, binding. Virus containing LANA abolished for DNA binding was incapable of viable latent infection in mice. Virus with mutations at the charged patch periphery exhibited substantial deficiency in expansion of latent infection, while central region substitutions had little effect. This deficiency was independent of BRD4. These results elucidate the LANA DNA binding domain structure and reveal a unique charged region that exerts a critical role in viral latent infection, likely acting through a host cell protein(s).

Crystal Structure of the Gamma-2 Herpesvirus LANA DNA Binding Domain Identifies Charged Surface Residues Which Impact Viral Latency.,Correia B, Cerqueira SA, Beauchemin C, Pires de Miranda M, Li S, Ponnusamy R, Rodrigues L, Schneider TR, Carrondo MA, Kaye KM, Simas JP, McVey CE PLoS Pathog. 2013 Oct;9(10):e1003673. doi: 10.1371/journal.ppat.1003673. Epub, 2013 Oct 17. PMID:24146618<ref>PMID:24146618</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4blg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Murid gammaherpesvirus 4]]
[[Category: Beauchemin C]]
[[Category: Carrondo MA]]
[[Category: Cerqueira SA]]
[[Category: Correia B]]
[[Category: Kaye KM]]
[[Category: Li S]]
[[Category: McVey CE]]
[[Category: Pires De Miranda M]]
[[Category: Ponnusamy R]]
[[Category: Rodrigues L]]
[[Category: Schneider TR]]
[[Category: Simas JP]]