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Article

Structural distortion of p53 by the mutation R249S and its rescue by a designed peptide: implications for "mutant conformation".

Journal of molecular biology - 6 Feb 2004

Friedler Assaf, DeDecker Brian S, Freund Stefan M V, Blair Caroline, Rüdiger Stefan, Fersht Alan R

Abstract excerpt

Missense mutations in the DNA-binding core domain of the tumour suppressor protein p53 are frequent in cancer. Many of them result in loss of native structure. The mutation R249S is one of the six most common cancer-associated p53 mutations ("hot-spots"). As it is highly frequent in hepatocellular carcinoma, its rescue is an important therapeutic target. We have used NMR techniques to study the structural effects...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 14741214
DOI: 10.1016/j.jmb.2003.12.005

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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