4l7l

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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=4l7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l7l RCSB], [http://www.ebi.ac.uk/pdbsum/4l7l 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=4l7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l7l RCSB], [http://www.ebi.ac.uk/pdbsum/4l7l PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/PARP3_HUMAN PARP3_HUMAN]] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.<ref>PMID:16924674</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 14:32, 24 December 2014

Human artd3 (parp3) - catalytic domain in complex with inhibitor ME0368

4l7l, resolution 2.10Å

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