4.3 Review

Structural aspects of multi-domain RING/Ubox E3 ligases in DNA repair

Journal

DNA REPAIR
Volume 8, Issue 4, Pages 525-535

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.dnarep.2009.01.014

Keywords

Ubiquitin; RING finger; Ubox; Ubiquitin ligase; Ligase structure; DNA repair

Funding

  1. EU-TMR
  2. EU-NOE Rubicon
  3. [KWF-NKI-2006-3476]

Ask authors/readers for more resources

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. (C) 2009 Elsevier BY. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.3
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available