2ilr
From Proteopedia
(New page: 200px<br /> <applet load="2ilr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ilr, resolution 2.00Å" /> '''Crystal structure o...) |
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| - | [[Image:2ilr. | + | [[Image:2ilr.jpg|left|200px]]<br /><applet load="2ilr" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2ilr, resolution 2.00Å" /> | caption="2ilr, resolution 2.00Å" /> | ||
'''Crystal structure of human Fanconi Anemia protein E C-terminal domain'''<br /> | '''Crystal structure of human Fanconi Anemia protein E C-terminal domain'''<br /> | ||
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==Overview== | ==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. | 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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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Fanconi anemia, complementation group E OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600901 600901]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2ILR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2ILR is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: helical repeat]] | [[Category: helical repeat]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:30:53 2008'' |
Revision as of 13:30, 23 January 2008
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Crystal structure of human Fanconi Anemia protein E C-terminal domain
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.
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
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