1. Structural aspects of multi-domain RING/Ubox E3 ligases in DNA repair
- Author
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Richard G. Hibbert, Francesca Mattiroli, and Titia K. Sixma
- Subjects
Magnetic Resonance Spectroscopy ,DNA Repair ,DNA damage ,DNA repair ,Ubiquitin-Protein Ligases ,Computational biology ,Ring (chemistry) ,Biochemistry ,Substrate Specificity ,chemistry.chemical_compound ,Ubiquitin ,Ring finger ,medicine ,Humans ,Molecular Biology ,biology ,Ubiquitination ,DNA ,Cell Biology ,Ubiquitin ligase ,medicine.anatomical_structure ,chemistry ,Ubiquitin-Conjugating Enzymes ,Domain (ring theory) ,biology.protein ,Protein Multimerization ,RING Finger Domains ,DNA Damage - Abstract
Ubiquitin conjugation plays critical roles in virtually all DNA repair pathways. This review provides an overview of the known multi-domain RING/Ubox E3 ligases and their domain structures. An analysis of known RING/Ubox X-ray and NMR structures leads to a discussion of the effects of dimerization. Structural and mechanistic data relating to the E3 ligase preferences for E2 interaction and chain-type specificity are reviewed and the role of the E3 ligases in regulation of the repair pathways is discussed.
- Published
- 2009
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