| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1981315 | DNA Repair | 2009 | 11 Pages |
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.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Richard G. Hibbert, Francesca Mattiroli, Titia K. Sixma,