2iqc | pdb_00002iqc
Crystal structure of Human FancF Protein that Functions in the Assembly of a DNA Damage Signaling Complex
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Overview
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.
Disease
Known disease associated with this structure: Fanconi anemia, complementation group F OMIM:[603467]
About this Structure
2IQC is a Single protein structure of sequence from Homo sapiens with HG as ligand. Full crystallographic information is available from OCA.
Reference
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, J Biol Chem. 2007 Jan 19;282(3):2047-55. Epub 2006 Nov 1. PMID:17082180
Page seeded by OCA on Mon Nov 12 22:46:59 2007
