3kjd: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: {{Seed}} left|200px <!-- The line below this paragraph, containing "STRUCTURE_3kjd", creates the "Structure Box" on the page. You may change the PDB parameter (which se...
 
No edit summary
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:3kjd.jpg|left|200px]]


<!--
==Human poly(ADP-ribose) polymerase 2, catalytic fragment in complex with an inhibitor ABT-888==
The line below this paragraph, containing "STRUCTURE_3kjd", creates the "Structure Box" on the page.
<StructureSection load='3kjd' size='340' side='right'caption='[[3kjd]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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='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>
{{STRUCTURE_3kjd|  PDB=3kjd  |  SCENE= }}
<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>
</table>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kj/3kjd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=3kjd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===Human poly(ADP-ribose) polymerase 2, catalytic fragment in complex with an inhibitor ABT-888===
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<ref>PMID:20092359</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3kjd" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
3KJD is a 2 chains structure of sequences from [http://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].
*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[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: SGC, Structural Genomics Consortium.]]
[[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: Alternative splicing]]
[[Category: Catalytic fragment]]
[[Category: Dna-binding]]
[[Category: Enzyme-inhibitor complex]]
[[Category: Glycosyltransferase]]
[[Category: Nad]]
[[Category: Nucleus]]
[[Category: Polymorphism]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 18 20:25:07 2009''

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"