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Article

Impact of low-frequency hotspot mutation R282Q on the structure of p53 DNA-binding domain as revealed by crystallography at 1.54 angstroms resolution.

Acta crystallographica. Section D, Biological crystallography - 1 May 2008

Tu Chao, Tan Yu Hong, Shaw Gary, Zhou Zheng, Bai Yawen, Luo Ray, Ji Xinhua

Abstract excerpt

Tumor suppressor p53 is a sequence-specific DNA-binding protein and its central DNA-binding domain (DBD) harbors six hotspots (Arg175, Gly245, Arg248, Arg249, Arg273 and Arg282) for human cancers. Here, the crystal structure of a low-frequency hotspot mutant, p53DBD(R282Q), is reported at 1.54 angstroms resolution together with the results of molecular-dynamics simulations on the basis of the structure. In...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 18453682
DOI: 10.1107/S0907444908003338
PMCID: PMC2631104

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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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