Structural aspects of multi-domain RING/Ubox E3 ligases in DNA repair.
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.
Hibbert
Richard G
RG
Division of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Mattiroli
Francesca
F
Sixma
Titia K
TK
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
D004247:DNA; D044763:Ubiquitin-Conjugating Enzymes; D044767:Ubiquitin-Protein Ligases