2ilr: Difference between revisions

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==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.

==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==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Nookala, R.K.]]

[[Category: Nookala, R K.]]

[[Category: Pellegrini, L.]]

[[Category: antiparallel helical hairpin]]

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[[Category: helical repeat]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:53:49 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+==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==
@@ Line 13: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Nookala, R.K.]]
+[[Category: Nookala, R K.]]
 [[Category: Pellegrini, L.]]
 [[Category: antiparallel helical hairpin]]
@@ Line 19: / Line 22: @@
 [[Category: helical repeat]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:30:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:53:49 2008''