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

Ambrose R Cole, Laurence P C Lewis, Helen Walden (Lead / Corresponding author)

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    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.

    Original languageEnglish
    Pages (from-to)294-298
    Number of pages5
    JournalNature Structural & Molecular Biology
    Volume17
    Issue number3
    DOIs
    Publication statusPublished - Mar 2010

    Keywords

    • GENE
    • KINETOCHORE
    • DNA-REPAIR
    • E2
    • PROTEIN
    • MONOUBIQUITINATED FANCD2
    • RECOGNITION
    • UBIQUITIN LIGASE
    • DOMAIN
    • CRYSTAL-STRUCTURE

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