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| | <StructureSection load='1gs0' size='340' side='right'caption='[[1gs0]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1gs0' size='340' side='right'caption='[[1gs0]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gs0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GS0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gs0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GS0 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></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]] 2.8Å</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=1gs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gs0 OCA], [https://pdbe.org/1gs0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gs0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gs0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gs0 ProSAT]</span></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=1gs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gs0 OCA], [https://pdbe.org/1gs0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gs0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gs0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gs0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PARP2_MOUSE PARP2_MOUSE]] 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_MOUSE PARP2_MOUSE] 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]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Oliver, A W]] | + | [[Category: Oliver AW]] |
| - | [[Category: Pearl, L H]] | + | [[Category: Pearl LH]] |
| - | [[Category: Roe, S M]] | + | [[Category: Roe SM]] |
| - | [[Category: Catalytic fragment]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Polymerase transferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PARP2_MOUSE 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) polymerase-1 (PARP-1) has become an important pharmacological target in the treatment of cancer due to its cellular role as a 'DNA-strand break sensor', which leads in part to resistance to some existing chemo- and radiological treatments. Inhibitors have now been developed which prevent PARP-1 from synthesizing poly(ADP-ribose) in response to DNA-breaks and potentiate the cytotoxicity of DNA damaging agents. However, with the recent discoveries of PARP-2, which has a similar DNA-damage dependent catalytic activity, and additional members containing the 'PARP catalytic' signature, the isoform selectivity and resultant pharmacological effects of existing inhibitors are brought into question. We present here the crystal structure of the catalytic fragment of murine PARP-2, at 2.8 A resolution, and compare this to the catalytic fragment of PARP-1, with an emphasis on providing a possible framework for rational drug design in order to develop future isoform-specific inhibitors.
Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2.,Oliver AW, Ame JC, Roe SM, Good V, de Murcia G, Pearl LH Nucleic Acids Res. 2004 Jan 22;32(2):456-64. Print 2004. PMID:14739238[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oliver AW, Ame JC, Roe SM, Good V, de Murcia G, Pearl LH. Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2. Nucleic Acids Res. 2004 Jan 22;32(2):456-64. Print 2004. PMID:14739238 doi:10.1093/nar/gkh215
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