The effects of phosphomimetic lid mutation on the thermostability of the N-terminal domain of MDM2.

@article{Worrall2010TheEO,
  title={The effects of phosphomimetic lid mutation on the thermostability of the N-terminal domain of MDM2.},
  author={Erin G. Worrall and Liam Worrall and Elizabeth Blackburn and Malcolm Walkinshaw and Ted R. Hupp},
  journal={Journal of molecular biology},
  year={2010},
  volume={398 3},
  pages={414-28}
}
The multidomain E3 ubiquitin ligase MDM2 catalyzes p53 ubiquitination by a "dual-site" docking mechanism whereby MDM2 binding to at least two distinct peptide motifs on p53 promotes ubiquitination. One protein-protein interaction occurs between the N-terminal hydrophobic pocket of MDM2 and the transactivation motif of p53, and the second interaction occurs between the acidic domain of MDM2 and a motif in the DNA-binding domain of p53. A flexible N-terminal pseudo-substrate or "lid" adjacent to… CONTINUE READING