4r6e: Difference between revisions

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'''Unreleased structure'''
==Human artd1 (parp1) - catalytic domain in complex with inhibitor niraparib==
 
<StructureSection load='4r6e' size='340' side='right' caption='[[4r6e]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
The entry 4r6e is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4r6e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R6E FirstGlance]. <br>
Authors: Karlberg, T., Thorsell, A.G., Brock, J., Schuler, H.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3JD:2-{4-[(3S)-PIPERIDIN-3-YL]PHENYL}-2H-INDAZOLE-7-CARBOXAMIDE'>3JD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4und|4und]], [[4uxb|4uxb]], [[4r5w|4r5w]]</td></tr>
Description: Human artd1 (parp1) -catalytic domain in complex with inhibitor niraparib
<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>
[[Category: Unreleased Structures]]
<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=4r6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r6e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r6e RCSB], [http://www.ebi.ac.uk/pdbsum/4r6e PDBsum]</span></td></tr>
</table>
== Function ==
[[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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brock, J]]
[[Category: Brock, J]]
[[Category: Thorsell, A.G]]
[[Category: Karlberg, T]]
[[Category: Schuler, H]]
[[Category: Schuler, H]]
[[Category: Karlberg, T]]
[[Category: Thorsell, A G]]
[[Category: Adp-ribosyl transferase]]
[[Category: Adp-ribosylation]]
[[Category: Dna repair]]
[[Category: Transferase-transferase inhibitor complex]]
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