4av1

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4av1]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AV1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4av1]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AV1 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uk0|1uk0]], [[1uk1|1uk1]], [[1wok|1wok]], [[2cok|2cok]], [[2cr9|2cr9]], [[2cs2|2cs2]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uk0|1uk0]], [[1uk1|1uk1]], [[1wok|1wok]], [[2cok|2cok]], [[2cr9|2cr9]], [[2cs2|2cs2]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr>
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<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=4av1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4av1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4av1 RCSB], [http://www.ebi.ac.uk/pdbsum/4av1 PDBsum]</span></td></tr>
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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=4av1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4av1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4av1 RCSB], [http://www.ebi.ac.uk/pdbsum/4av1 PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PARP1_HUMAN PARP1_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. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.<ref>PMID:17177976</ref> <ref>PMID:18172500</ref> <ref>PMID:19344625</ref> <ref>PMID:19661379</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks.,Ali AA, Timinszky G, Arribas-Bosacoma R, Kozlowski M, Hassa PO, Hassler M, Ladurner AG, Pearl LH, Oliver AW Nat Struct Mol Biol. 2012 Jun 10;19(7):685-92. doi: 10.1038/nsmb.2335. PMID:22683995<ref>PMID:22683995</ref>
The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks.,Ali AA, Timinszky G, Arribas-Bosacoma R, Kozlowski M, Hassa PO, Hassler M, Ladurner AG, Pearl LH, Oliver AW Nat Struct Mol Biol. 2012 Jun 10;19(7):685-92. doi: 10.1038/nsmb.2335. PMID:22683995<ref>PMID:22683995</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ali, A A.E.]]
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[[Category: Ali, A A.E]]
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[[Category: Arribas-Bosacoma, R.]]
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[[Category: Arribas-Bosacoma, R]]
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[[Category: Hassa, P O.]]
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[[Category: Hassa, P O]]
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[[Category: Hassler, M.]]
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[[Category: Hassler, M]]
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[[Category: Kozlowski, M.]]
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[[Category: Kozlowski, M]]
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[[Category: Ladurner, A G.]]
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[[Category: Ladurner, A G]]
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[[Category: Oliver, A W.]]
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[[Category: Oliver, A W]]
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[[Category: Pearl, L H.]]
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[[Category: Pearl, L H]]
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[[Category: Timinszky, G.]]
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[[Category: Timinszky, G]]
[[Category: Cancer]]
[[Category: Cancer]]
[[Category: Dbd]]
[[Category: Dbd]]

Revision as of 21:55, 25 December 2014

Crystal structure of the human PARP-1 DNA binding domain in complex with DNA

4av1, resolution 3.10Å

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