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[[Image:4epp.jpg|left|200px]]
==Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.==
<StructureSection load='4epp' size='340' side='right' caption='[[4epp]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4epp]] is a 2 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=4EPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EPP FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4epq|4epq]]</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=4epp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4epp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4epp RCSB], [http://www.ebi.ac.uk/pdbsum/4epp 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_4epp|  PDB=4epp  |  SCENE=  }}
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>


===Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_22673905}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[4epp]] is a 2 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=4EPP OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:022673905</ref><references group="xtra"/>
[[Category: Tetrahymena thermophila]]
[[Category: Tetrahymena thermophila]]
[[Category: Dunstan, M S.]]
[[Category: Dunstan, M S.]]
Retrieved from "https://proteopedia.org/4epp"