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==Human poly(ADP-ribose) polymerase 2, catalytic fragment in complex with an inhibitor ABT-888== | ==Human poly(ADP-ribose) polymerase 2, catalytic fragment in complex with an inhibitor ABT-888== | ||
<StructureSection load='3kjd' size='340' side='right' caption='[[3kjd]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='3kjd' size='340' side='right' caption='[[3kjd]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3kjd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3kjd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KJD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=78P:(2R)-2-(7-CARBAMOYL-1H-BENZIMIDAZOL-2-YL)-2-METHYLPYRROLIDINIUM'>78P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=78P:(2R)-2-(7-CARBAMOYL-1H-BENZIMIDAZOL-2-YL)-2-METHYLPYRROLIDINIUM'>78P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kcz|3kcz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kcz|3kcz]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADPRT2, ADPRTL2, PARP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADPRT2, ADPRTL2, PARP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<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> | <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> | ||
<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=3kjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kjd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kjd RCSB], [http://www.ebi.ac.uk/pdbsum/3kjd PDBsum]</span></td></tr> | <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=3kjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kjd OCA], [http://pdbe.org/3kjd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kjd RCSB], [http://www.ebi.ac.uk/pdbsum/3kjd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kjd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kjd ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3kjd" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Berg, S Van Den]] | [[Category: Berg, S Van Den]] | ||
Revision as of 17:27, 5 August 2016
Human poly(ADP-ribose) polymerase 2, catalytic fragment in complex with an inhibitor ABT-888Human poly(ADP-ribose) polymerase 2, catalytic fragment in complex with an inhibitor ABT-888
Structural highlights
Function[PARP2_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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPoly-ADP-ribose polymerases (PARPs) catalyze transfer of ADP-ribose from NAD(+) to specific residues in their substrate proteins or to growing ADP-ribose chains. PARP activity is involved in processes such as chromatin remodeling, transcription control, and DNA repair. Inhibitors of PARP activity may be useful in cancer therapy. PARP2 is the family member that is most similar to PARP1, and the two can act together as heterodimers. We used X-ray crystallography to determine two structures of the catalytic domain of human PARP2: the complexes with PARP inhibitors 3-aminobenzamide and ABT-888. These results contribute to our understanding of structural features and compound properties that can be employed to develop selective inhibitors of human ADP-ribosyltransferases. Crystal structure of the catalytic domain of human PARP2 in complex with PARP inhibitor ABT-888.,Karlberg T, Hammarstrom M, Schutz P, Svensson L, Schuler H Biochemistry. 2010 Feb 16;49(6):1056-8. PMID:20092359[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Human
- Arrowsmith, C H
- Berg, S Van Den
- Berglund, H
- Bountra, C
- Collins, R
- Edwards, A M
- Flodin, S
- Flores, A
- Graslund, S
- Hammarstrom, M
- Johansson, A
- Johansson, I
- Kallas, A
- Karlberg, T
- Kotenyova, T
- Kotzsch, A
- Kraulis, P
- Moche, M
- Nielsen, T K
- Nordlund, P
- Nyman, T
- Persson, C
- Roos, A K
- Structural genomic
- Schuler, H
- Schutz, P
- Siponen, M I
- Thorsell, A G
- Tresaugues, L
- Weigelt, J
- Welin, M
- Wisniewska, M
- Catalytic fragment
- Dna-binding
- Enzyme-inhibitor complex
- Glycosyltransferase
- Nad
- Nucleus
- Sgc
- Transferase