4rv6

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'''Unreleased structure'''
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==Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib==
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<StructureSection load='4rv6' size='340' side='right' caption='[[4rv6]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
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The entry 4rv6 is ON HOLD until Paper Publication
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4rv6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RV6 FirstGlance]. <br>
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Authors: Karlberg, T., Thorsell, A.G., 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=RPB:RUCAPARIB'>RPB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4und|4und]], [[4uxb|4uxb]], [[4r5w|4r5w]], [[4r6e|4r6e]]</td></tr>
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Description: Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib
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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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[[Category: Unreleased Structures]]
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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=4rv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv6 OCA], [http://pdbe.org/4rv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rv6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rv6 PDBsum]</span></td></tr>
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[[Category: Thorsell, A.G]]
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</table>
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[[Category: Schuler, H]]
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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: Karlberg, T]]
[[Category: Karlberg, T]]
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[[Category: Schuler, H]]
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[[Category: Thorsell, A G]]
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[[Category: Adp-ribosyl transferase]]
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[[Category: Adp-ribosylation]]
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[[Category: Transferase-transferase inhibitor complex]]

Revision as of 13:46, 9 December 2015

Human ARTD1 (PARP1) catalytic domain in complex with inhibitor Rucaparib

4rv6, resolution 3.19Å

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