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==Crystal structure of EBV tegument protein BNRF1 in complex with histone chaperone DAXX and histones H3.3-H4==
<StructureSection load='5kdm' size='340' side='right'caption='[[5kdm]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kdm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Epstein-barr_virus_strain_ag876 Epstein-barr virus strain ag876] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KDM 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]] 3.5&#8491;</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=5kdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kdm OCA], [https://pdbe.org/5kdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kdm RCSB], [https://www.ebi.ac.uk/pdbsum/5kdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kdm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H33_HUMAN H33_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The histone H3.3 chaperone DAXX is implicated in formation of heterochromatin and transcription silencing, especially for newly infecting DNA virus genomes entering the nucleus. Epstein-Barr virus (EBV) can efficiently establish stable latent infection as a chromatinized episome in the nucleus of infected cells. The EBV tegument BNRF1 is a DAXX-interacting protein required for the establishment of selective viral gene expression during latency. Here we report the structure of BNRF1 DAXX-interaction domain (DID) in complex with DAXX histone-binding domain (HBD) and histones H3.3-H4. BNRF1 DID contacts DAXX HBD and histones through non-conserved loops. The BNRF1-DAXX interface is responsible for BNRF1 localization to PML-nuclear bodies typically associated with host-antiviral resistance and transcriptional repression. Paradoxically, the interface is also required for selective transcription activation of viral latent cycle genes required for driving B-cell proliferation. These findings reveal molecular details of virus reprogramming of an antiviral histone chaperone to promote viral latency and cellular immortalization.

Structural basis underlying viral hijacking of a histone chaperone complex.,Huang H, Deng Z, Vladimirova O, Wiedmer A, Lu F, Lieberman PM, Patel DJ Nat Commun. 2016 Sep 1;7:12707. doi: 10.1038/ncomms12707. PMID:27581705<ref>PMID:27581705</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kdm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Death-associated protein 3D structures|Death-associated protein 3D structures]]
*[[Histone 3D structures|Histone 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Epstein-barr virus strain ag876]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Huang H]]
[[Category: Patel D]]