2ILR

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

Summary for 2ILR

• Entry DOI: 10.2210/pdb2ilr/pdb
• Descriptor: Fanconi anemia group E protein (2 entities in total)
• Functional Keywords: antiparallel helical hairpin, helical repeat, fanc repeat, oncoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9HB96
• Total number of polymer chains: 1
• Total formula weight: 28986.13

Authors

Pellegrini, L.,Nookala, R.K. (deposition date: 2006-10-03, release date: 2007-02-27, Last modification date: 2024-05-29)

Primary citation

Nookala, R.K.,Hussain, S.,Pellegrini, L.
Insights into Fanconi Anaemia from the structure of human FANCE
Nucleic Acids Res., 35:1638-1648, 2007

PubMed Abstract: 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.

PubMed: 17308347
DOI: 10.1093/nar/gkm033

Experimental method

X-RAY DIFFRACTION (2 Å)