2ilr

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{{Seed}}
 
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[[Image:2ilr.png|left|200px]]
 
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==Crystal structure of human Fanconi Anemia protein E C-terminal domain==
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The line below this paragraph, containing "STRUCTURE_2ilr", creates the "Structure Box" on the page.
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<StructureSection load='2ilr' size='340' side='right'caption='[[2ilr]], [[Resolution|resolution]] 2.00&Aring;' 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'>[[2ilr]] 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=2ILR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ILR 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">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=2ilr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ilr OCA], [https://pdbe.org/2ilr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ilr RCSB], [https://www.ebi.ac.uk/pdbsum/2ilr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ilr ProSAT]</span></td></tr>
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{{STRUCTURE_2ilr| PDB=2ilr | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/FANCE_HUMAN FANCE_HUMAN] Defects in FANCE are a cause of Fanconi anemia complementation group E (FANCE) [MIM:[https://omim.org/entry/600901 600901]. A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.<ref>PMID:11001585</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/FANCE_HUMAN FANCE_HUMAN] As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2.<ref>PMID:12093742</ref> <ref>PMID:17296736</ref>
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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/il/2ilr_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=2ilr 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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Fanconi Anaemia (FA) is a cancer predisposition disorder characterized by spontaneous chromosome breakage and high cellular sensitivity to genotoxic agents. In response to DNA damage, a multi-subunit assembly of FA proteins, the FA core complex, monoubiquitinates the downstream FANCD2 protein. The FANCE protein plays an essential role in the FA process of DNA repair as the FANCD2-binding component of the FA core complex. Here we report a crystallographic and biological study of human FANCE. The first structure of a FA protein reveals the presence of a repeated helical motif that provides a template for the structural rationalization of other proteins defective in Fanconi Anaemia. The portion of FANCE defined by our crystallographic analysis is sufficient for interaction with FANCD2, yielding structural information into the mode of FANCD2 recruitment to the FA core complex. Disease-associated mutations disrupt the FANCE-FANCD2 interaction, providing structural insight into the molecular mechanisms of FA pathogenesis.
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===Crystal structure of human Fanconi Anemia protein E C-terminal domain===
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Insights into Fanconi Anaemia from the structure of human FANCE.,Nookala RK, Hussain S, Pellegrini L Nucleic Acids Res. 2007;35(5):1638-48. Epub 2007 Feb 18. PMID:17308347<ref>PMID:17308347</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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The line below this paragraph, {{ABSTRACT_PUBMED_17308347}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2ilr" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17308347 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17308347}}
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Fanconi anemia, complementation group E OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600901 600901]]
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==About this Structure==
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2ILR is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILR OCA].
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==Reference==
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<ref group="xtra">PMID:17308347</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Nookala, R K.]]
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[[Category: Large Structures]]
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[[Category: Pellegrini, L.]]
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[[Category: Nookala RK]]
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[[Category: Antiparallel helical hairpin]]
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[[Category: Pellegrini L]]
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[[Category: Fanc repeat]]
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[[Category: Helical repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:24:15 2009''
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Current revision

Crystal structure of human Fanconi Anemia protein E C-terminal domain

PDB ID 2ilr

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