Structural regulation of cullin-RING ubiquitin ligase complexes.

@article{Duda2011StructuralRO,
  title={Structural regulation of cullin-RING ubiquitin ligase complexes.},
  author={David M. Duda and Daniel A. Yaussy Charles T. Scott and Matthew F. Calabrese and Erik S. Zimmerman and Ning Zheng and Brenda A. Schulman},
  journal={Current opinion in structural biology},
  year={2011},
  volume={21 2},
  pages={257-64}
}
Cullin-RING ligases (CRLs) compose the largest class of E3 ubiquitin ligases. CRLs are modular, multisubunit enzymes, comprising interchangeable substrate receptors dedicated to particular Cullin-RING catalytic cores. Recent structural studies have revealed numerous ways in which CRL E3 ligase activities are controlled, including multimodal E3 ligase activation by covalent attachment of the ubiquitin-like protein NEDD8, inhibition of CRL assembly/activity by CAND1, and several mechanisms of… CONTINUE READING