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Article

High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.

Science (New York, N.Y.) - 15 Jul 1994

Clore G M, Omichinski J G, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn A M

Abstract excerpt

The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel beta sheet. One beta strand...

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Identifiers

PMID: 8023159
DOI: 10.1126/science.8023159

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

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