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Structural determinants of human FANCF protein that function in the assembly of a DNA damage signaling complex.

Fanconi anemia (FA) is a rare autosomal recessive and X-linked chromosomal instability disorder. At least eight FA proteins (FANCA, B, C, E, F, G, L, and M) form a nuclear core complex required for monoubiquitination of a downstream protein, FANCD2. The human FANCF protein reportedly functions as a molecular adaptor within the FA nuclear complex, bridging between the subcomplexes A:G and C:E. Our x-ray crystallographic studies of the C-terminal domain of FANCF reveal a helical repeat structure similar to the Cand1 regulator of the Cul1-Rbx1-Skp1-Fbox(Skp2) ubiquitin ligase complex. Two C-terminal loops of FANCF are essential for monoubiquitination of FANCD2 and normal cellular resistance to the DNA cross-linking agent mitomycin C. FANCF mutants bearing amino acid substitutions in this C-terminal surface fail to interact with other components of the FA complex, indicating that this surface is critical for the proper assembly of the FA core complex.

Pubmed ID: 17082180 RIS Download

Mesh terms: Amino Acid Sequence | DNA Damage | Dose-Response Relationship, Drug | Fanconi Anemia Complementation Group F Protein | Humans | Mitomycin | Models, Molecular | Molecular Sequence Data | Protein Binding | Protein Conformation | Protein Structure, Secondary | Protein Structure, Tertiary | Signal Transduction | Transcription Factors | Ubiquitin

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Associated grants

  • Agency: NIDDK NIH HHS, Id: 2P01DK50654
  • Agency: NIDDK NIH HHS, Id: 5R01DK43889
  • Agency: NHLBI NIH HHS, Id: 5R01HL52725
  • Agency: NIGMS NIH HHS, Id: GM52504

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