Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation.

@article{Kulikov2006BindingOP,
  title={Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation.},
  author={Roman Kulikov and Markus Winter and Christine Blattner},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 39},
  pages={28575-83}
}
The Mdm2 protein is the major regulator of the tumor suppressor protein p53. We show that the p53 protein associates both with the N-terminal and with the central domain of Mdm2. The central p53-binding site of Mdm2 encompasses amino acids 235-300. Binding of p53 to the central domain is significantly enhanced after phosphorylation of the central domain of Mdm2. The N-terminal and central domains of Mdm2 act synergistically in binding to p53. p53 mutants that have mutations in the… CONTINUE READING

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