2ilr
From Proteopedia
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| - | [[Image:2ilr.jpg|left|200px]] | + | [[Image:2ilr.jpg|left|200px]] |
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| - | '''Crystal structure of human Fanconi Anemia protein E C-terminal domain''' | + | {{Structure |
| + | |PDB= 2ilr |SIZE=350|CAPTION= <scene name='initialview01'>2ilr</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= FANCE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of human Fanconi Anemia protein E C-terminal domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2ILR is a [ | + | 2ILR is a [[Single protein]] 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]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17308347 17308347] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helical repeat]] | [[Category: helical repeat]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:31:01 2008'' |
Revision as of 15:31, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | FANCE (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 diseases 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 Thu Mar 20 17:31:01 2008
