Structure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation

@inproceedings{Lechtenberg2016StructureOA,
  title={Structure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation},
  author={Bernhard C. Lechtenberg and Akhil Rajput and Ruslan Sanishvili and Małgorzata K. Dobaczewska and Carl F Ware and Peter D Mace and Stefan J. Riedl},
  booktitle={Nature},
  year={2016}
}
Ubiquitination is a central process affecting all facets of cellular signalling and function. A critical step in ubiquitination is the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate or a growing ubiquitin chain, which is mediated by E3 ubiquitin ligases. RING-type E3 ligases typically facilitate the transfer of ubiquitin from the E2 directly to the substrate. The RING-between-RING (RBR) family of RING-type E3 ligases, however, breaks this paradigm by forming a… CONTINUE READING