1z00

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{{Seed}}
 
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[[Image:1z00.png|left|200px]]
 
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==Solution structure of the C-terminal domain of ERCC1 complexed with the C-terminal domain of XPF==
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The line below this paragraph, containing "STRUCTURE_1z00", creates the "Structure Box" on the page.
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<StructureSection load='1z00' size='340' side='right'caption='[[1z00]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1z00]] is a 2 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=1Z00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z00 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z00 OCA], [https://pdbe.org/1z00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z00 RCSB], [https://www.ebi.ac.uk/pdbsum/1z00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z00 ProSAT]</span></td></tr>
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{{STRUCTURE_1z00| PDB=1z00 | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ERCC1_HUMAN ERCC1_HUMAN] Defects in ERCC1 are the cause of cerebro-oculo-facio-skeletal syndrome type 4 (COFS4) [MIM:[https://omim.org/entry/610758 610758]. COFS is a degenerative autosomal recessive disorder of prenatal onset affecting the brain, eye and spinal cord. After birth, it leads to brain atrophy, hypoplasia of the corpus callosum, hypotonia, cataracts, microcornea, optic atrophy, progressive joint contractures and growth failure. Facial dysmorphism is a constant feature. Abnormalities of the skull, eyes, limbs, heart and kidney also occur.<ref>PMID:17273966</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/ERCC1_HUMAN ERCC1_HUMAN] Structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z0/1z00_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1z00 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The human ERCC1/XPF complex is a structure-specific endonuclease with defined polarity that participates in multiple DNA repair pathways. We report the heterodimeric structure of the C-terminal domains of both proteins responsible for ERCC1/XPF complex formation. Both domains exhibit the double helix-hairpin-helix motif (HhH)2, and they are related by a pseudo-2-fold symmetry axis. In the XPF domain, the hairpin of the second motif is replaced by a short turn. The ERCC1 domain folds properly only in the presence of the XPF domain, which implies a role for XPF as a scaffold for the folding of ERCC1. The intersubunit interactions are largely hydrophobic in nature. NMR titration data show that only the ERCC1 domain of the ERCC1/XPF complex is involved in DNA binding. On the basis of these findings, we propose a model for the targeting of XPF nuclease via ERCC1-mediated interactions in the context of nucleotide excision repair.
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===Solution structure of the C-terminal domain of ERCC1 complexed with the C-terminal domain of XPF===
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The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair.,Tripsianes K, Folkers G, Ab E, Das D, Odijk H, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R Structure. 2005 Dec;13(12):1849-58. PMID:16338413<ref>PMID:16338413</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1z00" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16338413}}, adds the Publication Abstract to the page
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16338413 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16338413}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1Z00 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z00 OCA].
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==Reference==
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The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair., Tripsianes K, Folkers G, Ab E, Das D, Odijk H, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R, Structure. 2005 Dec;13(12):1849-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16338413 16338413]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Ab, E.]]
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[[Category: Ab E]]
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[[Category: Boelens, R.]]
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[[Category: Boelens R]]
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[[Category: Das, D.]]
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[[Category: Das D]]
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[[Category: Folkers, G.]]
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[[Category: Folkers G]]
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[[Category: Hoeijmakers, J H.J.]]
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[[Category: Hoeijmakers JHJ]]
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[[Category: Jaspers, N G.J.]]
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[[Category: Jaspers NGJ]]
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[[Category: Kaptein, R.]]
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[[Category: Kaptein R]]
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[[Category: Odijk, H.]]
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[[Category: Odijk H]]
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[[Category: Tripsianes, K.]]
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[[Category: Tripsianes K]]
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[[Category: Helix-hairpin-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:48:59 2008''
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Current revision

Solution structure of the C-terminal domain of ERCC1 complexed with the C-terminal domain of XPF

PDB ID 1z00

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