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6hmn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==POLYADPRIBOSYL GLYCOSIDASE IN COMPLEX WITH PDD00014909== | |
| - | + | <StructureSection load='6hmn' size='340' side='right' caption='[[6hmn]], [[Resolution|resolution]] 2.87Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6hmn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HMN FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=70J:3-methyl-6-[[(1-methylcyclopropyl)amino]-bis(oxidanyl)-$l^{4}-sulfanyl]-1-(phenylmethyl)quinazoline-2,4-dione'>70J</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | [[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Poly(ADP-ribose)_glycohydrolase Poly(ADP-ribose) glycohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.143 3.2.1.143] </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=6hmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hmn OCA], [http://pdbe.org/6hmn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hmn RCSB], [http://www.ebi.ac.uk/pdbsum/6hmn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hmn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Brassington, C]] | [[Category: Brassington, C]] | ||
[[Category: Hassall, G]] | [[Category: Hassall, G]] | ||
| - | [[Category: Tucker, J | + | [[Category: Tucker, J A]] |
| + | [[Category: Competitive inhibitor]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 08:20, 14 November 2018
POLYADPRIBOSYL GLYCOSIDASE IN COMPLEX WITH PDD00014909
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