Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail.

@article{Hamilton2001StructureOA,
  title={Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail.},
  author={Kendra Hamilton and M J Ellison and Kathryn R. Barber and R Scott Williams and J. Torin Huzil and Sean McKenna and Christopher Ptak and Mark A. Glover and Gary S. Shaw},
  journal={Structure},
  year={2001},
  volume={9 10},
  pages={897-904}
}
BACKGROUND Ubiquitin-conjugating enzymes (E2s) are central enzymes involved in ubiquitin-mediated protein degradation. During this process, ubiquitin (Ub) and the E2 protein form an unstable E2-Ub thiolester intermediate prior to the transfer of ubiquitin to an E3-ligase protein and the labeling of a substrate for degradation. A series of complex interactions occur among the target substrate, ubiquitin, E2, and E3 in order to efficiently facilitate the transfer of the ubiquitin molecule… CONTINUE READING

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