Structural basis for non-covalent interaction between ubiquitin and the ubiquitin conjugating enzyme variant human MMS2.

@article{Lewis2006StructuralBF,
  title={Structural basis for non-covalent interaction between ubiquitin and the ubiquitin conjugating enzyme variant human MMS2.},
  author={Michael J. Lewis and Linda F Saltibus and David D. Hau and Wei Xiao and Leo Spyracopoulos},
  journal={Journal of biomolecular NMR},
  year={2006},
  volume={34 2},
  pages={89-100}
}
Modification of proteins by post-translational covalent attachment of a single, or chain, of ubiquitin molecules serves as a signaling mechanism for a number of regulatory functions in eukaryotic cells. For example, proteins tagged with lysine-63 linked polyubiquitin chains are involved in error-free DNA repair. The catalysis of lysine-63 linked… CONTINUE READING