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4und

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'''Unreleased structure'''
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==HUMAN ARTD1 (PARP1) - CATALYTIC DOMAIN IN COMPLEX WITH INHIBITOR BMN673==
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<StructureSection load='4und' size='340' side='right' caption='[[4und]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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The entry 4und is ON HOLD until Paper Publication
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4und]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UND FirstGlance]. <br>
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Authors: KARLBERG, T., THORSELL, A.G., EKBLAD, T., KLEPSCH, M., PINTO, A.F., TRESAUGUES, L., MOCHE, M., SCHULER, H.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2YQ:(8S,9R)-5-FLUORO-8-(4-FLUOROPHENYL)-9-(1-METHYL-1H-1,2,4-TRIAZOL-5-YL)-2,7,8,9-TETRAHYDRO-3H-PYRIDO[4,3,2-DE]PHTHALAZIN-3-ONE'>2YQ</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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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Description: HUMAN ARTD1 (PARP1) -CATALYTIC DOMAIN IN COMPLEX WITH INHIBITOR BMN673
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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=4und FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4und OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4und RCSB], [http://www.ebi.ac.uk/pdbsum/4und PDBsum]</span></td></tr>
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[[Category: Unreleased Structures]]
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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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Ekblad, T]]
[[Category: Ekblad, T]]
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[[Category: Thorsell, A.G]]
 
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[[Category: Tresaugues, L]]
 
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[[Category: Pinto, A.F]]
 
[[Category: Karlberg, T]]
[[Category: Karlberg, T]]
[[Category: Klepsch, M]]
[[Category: Klepsch, M]]
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[[Category: Schuler, H]]
 
[[Category: Moche, M]]
[[Category: Moche, M]]
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[[Category: Pinto, A F]]
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[[Category: Schuler, H]]
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[[Category: Thorsell, A G]]
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[[Category: Tresaugues, L]]
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[[Category: Adp-ribosylation]]
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[[Category: Dna repair]]
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[[Category: Protein-inhibitor complex]]
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[[Category: Transferase]]

Revision as of 15:21, 17 June 2015

HUMAN ARTD1 (PARP1) - CATALYTIC DOMAIN IN COMPLEX WITH INHIBITOR BMN673

4und, resolution 2.20Å

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