Display Settings:

Format

Send to:

Choose Destination

    J Biol Chem. 2007 Jan 19;282(3):2047-55. Epub 2006 Nov 1.

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

    Kowal P, Gurtan AM, Stuckert P, D'Andrea AD, Ellenberger T.

    Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.

    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.

    PMID: 17082180 [PubMed - indexed for MEDLINE]

    LinkOut - more resources

    Full Text Sources:

    Other Literature Sources:

    Medical:

    Molecular Biology Databases:

    Supplemental Content

    Click here to read

    Structures reported by this article

    Patient drug information

    • Mitomycin (Mutamycin®)

      Your doctor has ordered the drug mitomycin to help treat your illness. The drug is given by injection into a vein.