2ilr

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[[Image:2ilr.jpg|left|200px]]
[[Image:2ilr.jpg|left|200px]]
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{{Structure
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|PDB= 2ilr |SIZE=350|CAPTION= <scene name='initialview01'>2ilr</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_2ilr", creates the "Structure Box" on the page.
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|SITE=
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|GENE= FANCE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2ilr| PDB=2ilr | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ilr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ilr OCA], [http://www.ebi.ac.uk/pdbsum/2ilr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ilr RCSB]</span>
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'''Crystal structure of human Fanconi Anemia protein E C-terminal domain'''
'''Crystal structure of human Fanconi Anemia protein E C-terminal domain'''
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[[Category: Nookala, R K.]]
[[Category: Nookala, R K.]]
[[Category: Pellegrini, L.]]
[[Category: Pellegrini, L.]]
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[[Category: antiparallel helical hairpin]]
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[[Category: Antiparallel helical hairpin]]
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[[Category: fanc repeat]]
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[[Category: Fanc repeat]]
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[[Category: helical repeat]]
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[[Category: Helical repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:38:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:45:51 2008''
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Revision as of 04:38, 4 May 2008

Image:2ilr.jpg

Template:STRUCTURE 2ilr

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


Contents

Overview

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.

Disease

Known disease associated with this structure: Fanconi anemia, complementation group E OMIM:[600901]

About this Structure

2ILR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 07:38:00 2008

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OCA

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