View source for 5ega


==2009 H1N1 PA endonuclease domain in complex with an N-acylhydrazone inhibitor==
<StructureSection load='5ega' size='340' side='right'caption='[[5ega]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ega]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/California/04/2009(H1N1)) Influenza A virus (A/California/04/2009(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EGA 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]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GK0:3,4,5-TRIS(OXIDANYL)-~{N}-[(~{E})-[3,4,5-TRIS(OXIDANYL)PHENYL]METHYLIDENEAMINO]BENZAMIDE'>GK0</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=5ega FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ega OCA], [https://pdbe.org/5ega PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ega RCSB], [https://www.ebi.ac.uk/pdbsum/5ega PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ega ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C3W5S0_I09A0 C3W5S0_I09A0] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Influenza virus PA endonuclease has recently emerged as an attractive target for the development of novel antiviral therapeutics. This is an enzyme with divalent metal ion(s) (Mg(2+) or Mn(2+)) in its catalytic site: chelation of these metal cofactors is an attractive strategy to inhibit enzymatic activity. Here we report the activity of a series of N-acylhydrazones in an enzymatic assay with PA-Nter endonuclease, as well as in cell-based influenza vRNP reconstitution and virus yield assays. Several N-acylhydrazones were found to have promising anti-influenza activity in the low micromolar concentration range and good selectivity. Computational docking studies are carried on to investigate the key features that determine inhibition of the endonuclease enzyme by N-acylhydrazones. Moreover, we here describe the crystal structure of PA-Nter in complex with one of the most active inhibitors, revealing its interactions within the protein's active site.

N-acylhydrazone inhibitors of influenza virus PA endonuclease with versatile metal binding modes.,Carcelli M, Rogolino D, Gatti A, De Luca L, Sechi M, Kumar G, White SW, Stevaert A, Naesens L Sci Rep. 2016 Aug 11;6:31500. doi: 10.1038/srep31500. PMID:27510745<ref>PMID:27510745</ref>

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

==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Kumar G]]
[[Category: White SW]]