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Article

Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions.

Nucleic acids research - 1 Oct 2013

Eldar Amir, Rozenberg Haim, Diskin-Posner Yael, Rohs Remo, Shakked Zippora

Abstract excerpt

A p53 hot-spot mutation found frequently in human cancer is the replacement of R273 by histidine or cysteine residues resulting in p53 loss of function as a tumor suppressor. These mutants can be reactivated by the incorporation of second-site suppressor mutations. Here, we present high-resolution crystal structures of the p53 core domains of the cancer-related proteins, the rescued proteins and their complexes...

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Share to Crystallography, X-Ray
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Structure, Tertiary

Share to Suppression, Genetic

Share to Tumor Suppressor Protein p53

Source

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Identifiers

PMID: 23863845
DOI: 10.1093/nar/gkt630
PMCID: PMC3794590

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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