3ce0

From Proteopedia

(Difference between revisions)

Revision as of 19:12, 24 January 2018

Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor PJ34

Structural highlights

3ce0 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2pa9, 3c49, 3c4h
Gene:	PARP3, ADPRT3, ADPRTL3 (HUMAN)
Activity:	NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PARP3_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. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.^[1]

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) activate DNA repair mechanisms upon stress- and cytotoxin-induced DNA damage, and inhibition of PARP activity is a lead in cancer drug therapy. We present a structural and functional analysis of the PARP domain of human PARP-3 in complex with several inhibitors. Of these, KU0058948 is the strongest inhibitor of PARP-3 activity. The presented crystal structures highlight key features for potent inhibitor binding and suggest routes for creating isoenzyme-specific PARP inhibitors.

Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3.,Lehtio L, Jemth AS, Collins R, Loseva O, Johansson A, Markova N, Hammarstrom M, Flores A, Holmberg-Schiavone L, Weigelt J, Helleday T, Schuler H, Karlberg T J Med Chem. 2009 May 14;52(9):3108-11. PMID:19354255^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rouleau M, McDonald D, Gagne P, Ouellet ME, Droit A, Hunter JM, Dutertre S, Prigent C, Hendzel MJ, Poirier GG. PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery. J Cell Biochem. 2007 Feb 1;100(2):385-401. PMID:16924674 doi:10.1002/jcb.21051
↑ Lehtio L, Jemth AS, Collins R, Loseva O, Johansson A, Markova N, Hammarstrom M, Flores A, Holmberg-Schiavone L, Weigelt J, Helleday T, Schuler H, Karlberg T. Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3. J Med Chem. 2009 May 14;52(9):3108-11. PMID:19354255 doi:10.1021/jm900052j

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ce0"

@@ Line 1: / Line 1: @@
 ==Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor PJ34==
 <StructureSection load='3ce0' size='340' side='right' caption='[[3ce0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PARP3, ADPRT3, ADPRTL3 ([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='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=3ce0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ce0 OCA], [http://pdbe.org/3ce0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ce0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ce0 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=3ce0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ce0 OCA], [http://pdbe.org/3ce0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ce0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ce0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ce0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/3ce0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/3ce0_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 </div>
 <div class="pdbe-citations 3ce0" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Poly (ADP-ribose) polymerase|Poly (ADP-ribose) polymerase]]
 == References ==
 <references/>
@@ Line 69: / Line 67: @@
 [[Category: Weigelt, J]]
 [[Category: Welin, M]]
+[[Category: Alternative splicing]]
 [[Category: Catalytic fragment]]
 [[Category: Enzyme-inhibitor complex]]

3ce0

From Proteopedia

Revision as of 19:12, 24 January 2018

Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor PJ34

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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