2dmj

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(New page: 200px<br /><applet load="2dmj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dmj" /> '''Solution structure of the first zf-PARP doma...)
Current revision (18:44, 29 May 2024) (edit) (undo)
 
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[[Image:2dmj.gif|left|200px]]<br /><applet load="2dmj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2dmj" />
 
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'''Solution structure of the first zf-PARP domain of human Poly(ADP-ribose)polymerase-1'''<br />
 
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==About this Structure==
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==Solution structure of the first zf-PARP domain of human Poly(ADP-ribose)polymerase-1==
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2DMJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DMJ OCA].
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<StructureSection load='2dmj' size='340' side='right'caption='[[2dmj]]' scene=''>
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[[Category: Homo sapiens]]
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== Structural highlights ==
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[[Category: NAD(+) ADP-ribosyltransferase]]
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<table><tr><td colspan='2'>[[2dmj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DMJ FirstGlance]. <br>
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[[Category: Single protein]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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[[Category: Hayashi, F.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[Category: Nagashima, T.]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dmj OCA], [https://pdbe.org/2dmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dmj RCSB], [https://www.ebi.ac.uk/pdbsum/2dmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dmj ProSAT], [https://www.topsan.org/Proteins/RSGI/2dmj TOPSAN]</span></td></tr>
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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</table>
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[[Category: Yokoyama, S.]]
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== Function ==
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[[Category: ZN]]
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[https://www.uniprot.org/uniprot/PARP1_HUMAN PARP1_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. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.<ref>PMID:17177976</ref> <ref>PMID:18172500</ref> <ref>PMID:19344625</ref> <ref>PMID:19661379</ref>
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[[Category: adprt]]
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== Evolutionary Conservation ==
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[[Category: dna ligase iii]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: dna nick sensor]]
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Check<jmol>
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[[Category: dna repair]]
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<jmolCheckbox>
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[[Category: nad(+) adp-ribosyltransferase 1]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dm/2dmj_consurf.spt"</scriptWhenChecked>
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[[Category: national project on protein structural and functional analyses]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: nppsfa]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: parp-1]]
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</jmolCheckbox>
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[[Category: poly(adp-ribose) synthetase 1]]
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</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=2dmj ConSurf].
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[[Category: riken structural genomics/proteomics initiative]]
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<div style="clear:both"></div>
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[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: transcription]]
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[[Category: xrcc1]]
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[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:40:22 2007''
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==See Also==
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*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Hayashi F]]
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[[Category: Nagashima T]]
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[[Category: Yokoyama S]]

Current revision

Solution structure of the first zf-PARP domain of human Poly(ADP-ribose)polymerase-1

PDB ID 2dmj

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