1gs0: Difference between revisions

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-{{Seed}}
-[[Image:1gs0.png|left|200px]]
-<!--
+==Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2==
-The line below this paragraph, containing "STRUCTURE_1gs0", creates the "Structure Box" on the page.
+<StructureSection load='1gs0' size='340' side='right'caption='[[1gs0]], [[Resolution|resolution]] 2.80&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'>[[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>
-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]] 2.8&#8491;</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>
-{{STRUCTURE_1gs0|  PDB=1gs0  |  SCENE=  }}
+</table>
+== 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.
+== 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/gs/1gs0_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=1gs0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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===
+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<ref>PMID:14739238</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1gs0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_14739238}}, adds the Publication Abstract to the page
+*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 14739238 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14739238}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-GS0 is a 2 chains structure of sequences from [http://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].
-==Reference==
-<ref group="xtra">PMID:14739238</ref><references group="xtra"/>
 [[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: Crystal structure]]
-[[Category: Dna-binding]]
-[[Category: Nuclear protein]]
-[[Category: Polymerase transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:36:43 2009''