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Article

Molecular mechanism of the interaction between MDM2 and p53.

Journal of molecular biology - 25 Oct 2002

Schon Oliver, Friedler Assaf, Bycroft Mark, Freund Stefan M V, Fersht Alan R

Abstract excerpt

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....

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Source

Identifiers

PMID: 12381304
DOI: 10.1016/s0022-2836(02)00852-5

Genes

MDM2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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