View source for 9js5


==Crystal structure of the ASFV-derived histone-like protein pA104R==
<StructureSection load='9js5' size='340' side='right'caption='[[9js5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9js5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/African_swine_fever_virus African swine fever virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9JS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JS5 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9js5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9js5 OCA], [https://pdbe.org/9js5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9js5 RCSB], [https://www.ebi.ac.uk/pdbsum/9js5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9js5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0A1E0L7_ASF A0A0A1E0L7_ASF] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
African swine fever is a highly lethal disease caused by the African swine fever virus (ASFV), posing a significant threat to the global pig industry, wherease no approved treatments are currently available. The ASFV DNA-binding protein, pA104R, plays a critical role in viral genome packaging and replication, making it a key target for drug discovery. Through structure-based virtual screening, we identified a polyphenolic compound, thonningianin A, which disrupts the pA104R-DNA binding and significantly inhibits ASFV replication. Mechanistic study revealed that thonningianin A binds to the DNA-binding region of pA104R, forming strong hydrogen bonds with H100 and occupying the vital DNA-binding residues K92, R94, and K97. In addition, we resolved the high-resolution (1.8 A) structure of pA104R (PDB ID 9JS5), providing valuable insights for future drug screening. Together, these results demonstrate that thonningianin A holds great potential for the development of anti-ASFV drug, as a herb extract with favourable pharmacokinetic properties and safety.

Thonningianin A disrupts pA104R-DNA binding and inhibits African swine fever virus replication.,Li QJ, Shao HH, Zheng LL, Liu Q, Huo CC, Yi DR, Feng T, Cen S Emerg Microbes Infect. 2025 Dec;14(1):2482697. doi: , 10.1080/22221751.2025.2482697. Epub 2025 Apr 1. PMID:40138179<ref>PMID:40138179</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9js5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: African swine fever virus]]
[[Category: Large Structures]]
[[Category: Cen S]]
[[Category: Li Q]]
[[Category: Shao H]]
[[Category: Yi D]]