3kjd: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 1: Line 1:


==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]] 1.95&Aring;' scene=''>
<StructureSection load='3kjd' size='340' side='right'caption='[[3kjd]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[3kjd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kcz|3kcz]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kjd OCA], [https://pdbe.org/3kjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kjd RCSB], [https://www.ebi.ac.uk/pdbsum/3kjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kjd ProSAT]</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://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 ==
[[http://www.uniprot.org/uniprot/PARP2_HUMAN 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.  
[https://www.uniprot.org/uniprot/PARP2_HUMAN 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 33: Line 31:


==See Also==
==See Also==
*[[Poly (ADP-ribose) polymerase|Poly (ADP-ribose) polymerase]]
*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H]]
[[Category: Large Structures]]
[[Category: Berg, S Van Den]]
[[Category: Arrowsmith CH]]
[[Category: Berglund, H]]
[[Category: Berglund H]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Collins, R]]
[[Category: Collins R]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Flodin, S]]
[[Category: Flodin S]]
[[Category: Flores, A]]
[[Category: Flores A]]
[[Category: Graslund, S]]
[[Category: Graslund S]]
[[Category: Hammarstrom, M]]
[[Category: Hammarstrom M]]
[[Category: Johansson, A]]
[[Category: Johansson A]]
[[Category: Johansson, I]]
[[Category: Johansson I]]
[[Category: Kallas, A]]
[[Category: Kallas A]]
[[Category: Karlberg, T]]
[[Category: Karlberg T]]
[[Category: Kotenyova, T]]
[[Category: Kotenyova T]]
[[Category: Kotzsch, A]]
[[Category: Kotzsch A]]
[[Category: Kraulis, P]]
[[Category: Kraulis P]]
[[Category: Moche, M]]
[[Category: Moche M]]
[[Category: Nielsen, T K]]
[[Category: Nielsen TK]]
[[Category: Nordlund, P]]
[[Category: Nordlund P]]
[[Category: Nyman, T]]
[[Category: Nyman T]]
[[Category: Persson, C]]
[[Category: Persson C]]
[[Category: Roos, A K]]
[[Category: Roos AK]]
[[Category: Structural genomic]]
[[Category: Schuler H]]
[[Category: Schuler, H]]
[[Category: Schutz P]]
[[Category: Schutz, P]]
[[Category: Siponen MI]]
[[Category: Siponen, M I]]
[[Category: Thorsell AG]]
[[Category: Thorsell, A G]]
[[Category: Tresaugues L]]
[[Category: Tresaugues, L]]
[[Category: Van Den Berg S]]
[[Category: Weigelt, J]]
[[Category: Weigelt J]]
[[Category: Welin, M]]
[[Category: Welin M]]
[[Category: Wisniewska, M]]
[[Category: Wisniewska M]]
[[Category: Catalytic fragment]]
[[Category: Dna-binding]]
[[Category: Enzyme-inhibitor complex]]
[[Category: Glycosyltransferase]]
[[Category: Nad]]
[[Category: Nucleus]]
[[Category: Sgc]]
[[Category: Transferase]]

Latest revision as of 19:13, 1 November 2023

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

3kjd is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Poly-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 Also

References

  1. ↑ Karlberg T, Hammarstrom M, Schutz P, Svensson L, Schuler H. Crystal structure of the catalytic domain of human PARP2 in complex with PARP inhibitor ABT-888. Biochemistry. 2010 Feb 16;49(6):1056-8. PMID:20092359 doi:10.1021/bi902079y

3kjd, resolution 1.95Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3kjd&oldid=3934756"