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[[Image:2riq.jpg|left|200px]]<br /><applet load="2riq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2riq, resolution 1.70&Aring;" />
'''Crystal Structure of the Third Zinc-binding domain of human PARP-1'''<br />


==Overview==
==Crystal Structure of the Third Zinc-binding domain of human PARP-1==
PARP-1 is a chromatin-associated enzyme with multiple cellular functions, including DNA repair, transcriptional regulation, and cell signaling., PARP-1 has a modular architecture with six independent domains comprising, the 113 kDa polypeptide. Two zinc-finger domains at the N-terminus of, PARP-1 bind to DNA and thereby activate the catalytic domain situated at, the C-terminus of the enzyme. The tight coupling of DNA binding and, catalytic activities is critical to the cellular regulation of PARP-1, function, however, the mechanism for coordinating these activities remains, an unsolved problem. Here, we demonstrate using spectroscopic and, crystallographic analysis that human PARP-1 has a third zinc-binding, domain. Biochemical mutagenesis and deletion analysis indicate that this, region mediates inter-domain contacts important for DNA-dependent enzyme, activation. The crystal structure of the third zinc-binding domain reveals, a zinc ribbon fold and suggests conserved residues that could form, inter-domain contacts. The new zinc-binding domain self-associates in the, crystal lattice to form a homodimer with a head-to-tail arrangement. The, structure of the homodimer provides a scaffold for assembling the, activated state of PARP-1 and suggests a mechanism for coupling the DNA, binding and catalytic functions of PARP-1.
<StructureSection load='2riq' size='340' side='right'caption='[[2riq]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2riq]] is a 1 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=2RIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RIQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2riq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2riq OCA], [https://pdbe.org/2riq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2riq RCSB], [https://www.ebi.ac.uk/pdbsum/2riq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2riq ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== 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/ri/2riq_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=2riq ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2RIQ 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 <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=EOH:'>EOH</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIQ OCA].
*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
 
== References ==
==Reference==
<references/>
A third zinc-binding domain of human PARP-1 coordinates DNA-dependent enzyme activation., Langelier MF, Servent KM, Rogers EE, Pascal JM, J Biol Chem. 2007 Nov 30;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18055453 18055453]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: NAD(+) ADP-ribosyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Langelier MF]]
[[Category: Langelier, M.F.]]
[[Category: Pascal JM]]
[[Category: Pascal, J.M.]]
[[Category: Servent KM]]
[[Category: Servent, K.M.]]
[[Category: EOH]]
[[Category: GOL]]
[[Category: ZN]]
[[Category: adp-ribosylation]]
[[Category: dna damage]]
[[Category: dna repair]]
[[Category: dna-binding]]
[[Category: glycosyltransferase]]
[[Category: metal-binding]]
[[Category: nad]]
[[Category: nucleus]]
[[Category: phosphorylation]]
[[Category: polymorphism]]
[[Category: transferase]]
[[Category: zinc]]
[[Category: zinc-finger]]
[[Category: zn finger]]
[[Category: zn ribbon]]
[[Category: zn-binding domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb  6 15:31:55 2008''

Latest revision as of 09:22, 21 February 2024

Crystal Structure of the Third Zinc-binding domain of human PARP-1

2riq, resolution 1.70Å

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