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4b1i

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<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=4b1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b1i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b1i RCSB], [http://www.ebi.ac.uk/pdbsum/4b1i PDBsum]</span></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=4b1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b1i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b1i RCSB], [http://www.ebi.ac.uk/pdbsum/4b1i PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PARG_HUMAN PARG_HUMAN]] Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters.<ref>PMID:23102699</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 19:50, 25 December 2014

Structure of human PARG catalytic domain in complex with OA-ADP-HPD

4b1i, resolution 2.14Å

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