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Article

Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain.

The EMBO journal - 15 Oct 1997

McCoy M, Stavridi E S, Waterman J L, Wieczorek A M, Opella S J, Halazonetis T D

Abstract excerpt

The p53 tumor suppressor oligomerization domain, a dimer of two primary dimers, is an independently folding domain whose subunits consist of a beta-strand, a tight turn and an alpha-helix. To evaluate the effect of hydrophobic side-chains on three-dimensional structure, we substituted residues Phe341 and Leu344 in the alpha-helix with other hydrophobic amino acids. Substitutions that resulted in residue 341...

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Source

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Identifiers

PMID: 9321402
DOI: 10.1093/emboj/16.20.6230
PMCID: PMC1326307

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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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