2IQC

Crystal structure of Human FancF Protein that Functions in the Assembly of a DNA Damage Signaling Complex

Summary for 2IQC

• Entry DOI: 10.2210/pdb2iqc/pdb
• Descriptor: Fanconi anemia group F protein, MERCURY (II) ION (3 entities in total)
• Functional Keywords: fanconi, heat-like repeat, dna-damage, complex subunit, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9NPI8
• Total number of polymer chains: 1
• Total formula weight: 23554.30

Authors

Kowal, P.,Gurtan, A.M.,Stuckert, P.,Lehmann, C.,D'Andrea, A.,Ellenberger, T.E. (deposition date: 2006-10-13, release date: 2006-11-07, Last modification date: 2024-02-21)

Primary citation

Kowal, P.,Gurtan, A.M.,Stuckert, P.,D'Andrea, A.D.,Ellenberger, T.
Structural determinants of human FANCF protein that function in the assembly of a DNA damage signaling complex.
J.Biol.Chem., 282:2047-2055, 2007

PubMed Abstract: 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: 17082180
DOI: 10.1074/jbc.M608356200

Experimental method

X-RAY DIFFRACTION (2.4 Å)