Molecular mechanism of the interaction between MDM2 and p53.

@article{Schon2002MolecularMO,
  title={Molecular mechanism of the interaction between MDM2 and p53.},
  author={Oliver Schon and Assaf Friedler and Mark Bycroft and Stefan Freund and A. R. Fersht},
  journal={Journal of molecular biology},
  year={2002},
  volume={323 3},
  pages={491-501}
}
We have investigated the kinetic and thermodynamic basis of the p53-MDM2 interaction using a set of peptides based on residues 15-29 of p53. Wild-type p53 peptide bound MDM2 with a dissociation constant of 580nM. Phosphorylation of S15 and S20 did not affect binding, but T18 phosphorylation weakened binding tenfold, indicating that phosphorylation of only T18 is responsible for abrogating p53-MDM2 binding. Truncation to residues 17-26 increased affinity 13-fold, but further truncation to 19-26… CONTINUE READING

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