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Article

Evidence for allosteric effects on p53 oligomerization induced by phosphorylation.

Protein science : a publication of the Protein Society - 1 Feb 2018

Muller Petr, Chan Juliana M, Simoncik Oliver, Fojta Miroslav, Lane David P, Hupp Ted, Vojtesek Borivoj

Abstract excerpt

p53 is a tetrameric protein with a thermodynamically unstable deoxyribonucleic acid (DNA)-binding domain flanked by intrinsically disordered regulatory domains that control its activity. The unstable and disordered segments of p53 allow high flexibility as it interacts with binding partners and permits a rapid on/off switch to control its function. The p53 tetramer can exist in multiple conformational states, any...

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Identifiers

PMID: 29124793
DOI: 10.1002/pro.3344
PMCID: PMC5775181

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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