2kn7

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==Structure of the XPF-single strand DNA complex==
==Structure of the XPF-single strand DNA complex==
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<StructureSection load='2kn7' size='340' side='right' caption='[[2kn7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2kn7' size='340' side='right'caption='[[2kn7]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2kn7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KN7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KN7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2kn7]] is a 4 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=2KN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KN7 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2aq0|2aq0]], [[1z00|1z00]]</td></tr>
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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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XPF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2kn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kn7 OCA], [https://pdbe.org/2kn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kn7 RCSB], [https://www.ebi.ac.uk/pdbsum/2kn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kn7 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kn7 OCA], [http://pdbe.org/2kn7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kn7 RCSB], [http://www.ebi.ac.uk/pdbsum/2kn7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kn7 ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/XPF_HUMAN XPF_HUMAN]] Defects in ERCC4 are the cause of xeroderma pigmentosum complementation group F (XP-F) [MIM:[http://omim.org/entry/278760 278760]]; also known as xeroderma pigmentosum VI (XP6). XP-F is an autosomal recessive disease characterized by hypersensitivity of the skin to sunlight followed by high incidence of skin cancer and frequent neurologic abnormalities.<ref>PMID:8797827</ref> <ref>PMID:9580660</ref> <ref>PMID:9579555</ref> Defects in ERCC4 are a cause of XFE progeroid syndrome (XFEPS) [MIM:[http://omim.org/entry/610965 610965]]. This syndrome is illustrated by one patient who presented with dwarfism, cachexia and microcephaly.<ref>PMID:17183314</ref>
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[https://www.uniprot.org/uniprot/XPF_HUMAN XPF_HUMAN] Defects in ERCC4 are the cause of xeroderma pigmentosum complementation group F (XP-F) [MIM:[https://omim.org/entry/278760 278760]; also known as xeroderma pigmentosum VI (XP6). XP-F is an autosomal recessive disease characterized by hypersensitivity of the skin to sunlight followed by high incidence of skin cancer and frequent neurologic abnormalities.<ref>PMID:8797827</ref> <ref>PMID:9580660</ref> <ref>PMID:9579555</ref> Defects in ERCC4 are a cause of XFE progeroid syndrome (XFEPS) [MIM:[https://omim.org/entry/610965 610965]. This syndrome is illustrated by one patient who presented with dwarfism, cachexia and microcephaly.<ref>PMID:17183314</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/XPF_HUMAN XPF_HUMAN]] Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link.<ref>PMID:19596235</ref>
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[https://www.uniprot.org/uniprot/XPF_HUMAN XPF_HUMAN] Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link.<ref>PMID:19596235</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2kn7 ConSurf].
</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=2kn7 ConSurf].
<div style="clear:both"></div>
<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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Human XPF/ERCC1 is a structure-specific DNA endonuclease that nicks the damaged DNA strand at the 5' end during nucleotide excision repair. We determined the structure of the complex of the C-terminal domain of XPF with 10 nt ssDNA. A positively charged region within the second helix of the first HhH motif contacts the ssDNA phosphate backbone. One guanine base is flipped out of register and positioned in a pocket contacting residues from both HhH motifs of XPF. Comparison to other HhH-containing proteins indicates a one-residue deletion in the second HhH motif of XPF that has altered the hairpin conformation, thereby permitting ssDNA interactions. Previous nuclear magnetic resonance studies showed that ERCC1 in the XPF-ERCC1 heterodimer can bind dsDNA. Combining the two observations gives a model that underscores the asymmetry of the human XPF/ERCC1 heterodimer in binding at an ss/ds DNA junction.
 
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The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition.,Das D, Folkers GE, van Dijk M, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R Structure. 2012 Apr 4;20(4):667-75. Epub 2012 Apr 3. PMID:22483113<ref>PMID:22483113</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 2kn7" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Endonuclease|Endonuclease]]
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Boelens, R]]
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[[Category: Large Structures]]
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[[Category: Das, D]]
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[[Category: Boelens R]]
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[[Category: Dijk, M van]]
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[[Category: Das D]]
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[[Category: Folkers, G E]]
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[[Category: Folkers GE]]
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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: Hhh]]
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[[Category: Van Dijk M]]
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[[Category: Hydrolase-dna complex]]
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[[Category: Ner]]
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[[Category: Protein-ssdna complex]]
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[[Category: Xpf/ercc1]]
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Current revision

Structure of the XPF-single strand DNA complex

PDB ID 2kn7

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