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The structure of the catalytic subunit FANCL of the Fanconi anemia core complex

DOI: 10.1038/nsmb.1759 DOI Help
PMID: 20154706 PMID Help

Authors: Charlotte Hodson (Cancer Research UK London Research Institute) , Ambrose Cole (Cancer Research UK London Research Institute) , Laurence Lewis (Cancer Research UK London Research Institute) , Helen Walden (Cancer Research UK)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Structural & Molecular Biology , VOL 17 (3) , PAGES 294–298

State: Published (Approved)
Published: February 2010

Abstract: The Fanconi anemia (FA) pathway is activated in response to DNA damage, leading to monoubiquitination of the substrates FANCI and FANCD2 by the FA core complex. Here we report the crystal structure of FANCL, the catalytic subunit of the FA core complex, at 3.2 Å. The structure reveals an architecture fundamentally different from previous sequence-based predictions. The molecule is composed of an N-terminal E2-like fold, which we term the ELF domain, a novel double-RWD (DRWD) domain, and a C-terminal really interesting new gene (RING) domain predicted to facilitate E2 binding. Binding assays show that the DRWD domain, but not the ELF domain, is responsible for substrate binding.

Journal Keywords: Catalytic; Crystallography; X-Ray; Drosophila; Fanconi; Fanconi; Protein; Secondary; Protein; Tertiary

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Added On: 16/03/2010 10:08

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