5kpp

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m (Protected "5kpp" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5kpp is ON HOLD
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==Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor==
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<StructureSection load='5kpp' size='340' side='right' caption='[[5kpp]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
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Authors: Cao, R., Wang, Y.L., Zhou, J., Huang, N., Xu, B.L.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5kpp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KPP FirstGlance]. <br>
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Description: Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6WZ:1-[[4-FLUORANYL-3-[(3R)-3-METHYL-4-[2,2,2-TRIS(FLUORANYL)ETHYL]PIPERAZIN-1-YL]CARBONYL-PHENYL]METHYL]QUINAZOLINE-2,4-DIONE'>6WZ</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kpn|5kpn]], [[5kpo|5kpo]], [[5kpq|5kpq]]</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 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=5kpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kpp OCA], [http://pdbe.org/5kpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kpp RCSB], [http://www.ebi.ac.uk/pdbsum/5kpp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kpp ProSAT]</span></td></tr>
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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>
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[[Category: Cao, R]]
[[Category: Huang, N]]
[[Category: Huang, N]]
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[[Category: Wang, Y.L]]
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[[Category: Wang, Y L]]
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[[Category: Cao, R]]
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[[Category: Xu, B L]]
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[[Category: Xu, B.L]]
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[[Category: Zhou, J]]
[[Category: Zhou, J]]
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[[Category: Complex]]
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[[Category: Inhibitor]]
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[[Category: Transferase-transferase inhibitor complex]]

Revision as of 18:36, 10 December 2016

Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor

5kpp, resolution 2.33Å

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