4epq: Difference between revisions
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[[ | ==canonical poly(ADP-ribose) glycohydrolase RBPI inhibitor complex from Tetrahymena thermophila== | ||
<StructureSection load='4epq' size='340' side='right' caption='[[4epq]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4epq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EPQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EPQ FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0RR:3-{(5Z)-5-[5-CHLORO-1-(2,6-DICHLOROBENZYL)-2-OXO-1,2-DIHYDRO-3H-INDOL-3-YLIDENE]-4-OXO-2-THIOXO-1,3-THIAZOLIDIN-3-YL}PROPANOIC+ACID'>0RR</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4epp|4epp]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4epq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4epq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4epq RCSB], [http://www.ebi.ac.uk/pdbsum/4epq PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Poly(ADP-ribosyl)ation is a reversible post-translational protein modification involved in the regulation of a number of cellular processes including DNA repair, chromatin structure, mitosis, transcription, checkpoint activation, apoptosis and asexual development. The reversion of poly(ADP-ribosyl)ation is catalysed by poly(ADP-ribose) (PAR) glycohydrolase (PARG), which specifically targets the unique PAR (1''-2') ribose-ribose bonds. Here we report the structure and mechanism of the first canonical PARG from the protozoan Tetrahymena thermophila. In addition, we reveal the structure of T. thermophila PARG in a complex with a novel rhodanine-containing mammalian PARG inhibitor RBPI-3. Our data demonstrate that the protozoan PARG represents a good model for human PARG and is therefore likely to prove useful in guiding structure-based discovery of new classes of PARG inhibitors. | |||
Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase.,Dunstan MS, Barkauskaite E, Lafite P, Knezevic CE, Brassington A, Ahel M, Hergenrother PJ, Leys D, Ahel I Nat Commun. 2012 Jun 6;3:878. doi: 10.1038/ncomms1889. PMID:22673905<ref>PMID:22673905</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Tetrahymena thermophila]] | [[Category: Tetrahymena thermophila]] | ||
[[Category: Dunstan, M S.]] | [[Category: Dunstan, M S.]] | ||
Revision as of 09:13, 11 June 2014
canonical poly(ADP-ribose) glycohydrolase RBPI inhibitor complex from Tetrahymena thermophila
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