5ega: Difference between revisions
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==2009 H1N1 PA endonuclease domain in complex with an N-acylhydrazone inhibitor== | |||
<StructureSection load='5ega' size='340' side='right' caption='[[5ega]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ega]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EGA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5des|5des]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ega FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ega OCA], [http://pdbe.org/5ega PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ega RCSB], [http://www.ebi.ac.uk/pdbsum/5ega PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ega ProSAT]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ega" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kumar, G]] | [[Category: Kumar, G]] | ||
[[Category: White, S W]] | |||
[[Category: Endonuclease]] | |||
[[Category: Hydrolase-hydrolase inhibitor complex]] | |||
[[Category: Influenza]] | |||
Revision as of 13:54, 10 September 2016
2009 H1N1 PA endonuclease domain in complex with an N-acylhydrazone inhibitor
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