title: Structural aspects of multi-domain RING/Ubox E3 ligases in DNA repair.
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.
authors.affiliation: Division of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
authors.forename: Richard G
authors.initials: RG
authors.lastname: Hibbert
authors.forename: Francesca
authors.initials: F
authors.lastname: Mattiroli
authors.forename: Titia K
authors.initials: TK
authors.lastname: Sixma
mesh_terms: D004247:DNA / Q000378:metabolism; D004249:DNA Damage; D004260:DNA Repair; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D055503:Protein Multimerization; D054829:RING Finger Domains; D013379:Substrate Specificity; D044763:Ubiquitin-Conjugating Enzymes / Q000737:chemistry / Q000502:physiology; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry / Q000502:physiology; D054875:Ubiquitination
chemical_list: D004247:DNA; D044763:Ubiquitin-Conjugating Enzymes; D044767:Ubiquitin-Protein Ligases