Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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 A. 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.
The structure of the catalytic subunit FANCL of the Fanconi anemia core complex.,Cole AR, Lewis LP, Walden H Nat Struct Mol Biol. 2010 Mar;17(3):294-8. Epub 2010 Feb 14. PMID:20154706[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cole AR, Lewis LP, Walden H. The structure of the catalytic subunit FANCL of the Fanconi anemia core complex. Nat Struct Mol Biol. 2010 Mar;17(3):294-8. Epub 2010 Feb 14. PMID:20154706 doi:10.1038/nsmb.1759
