Abstract
The p53 protein is a tetrameric transcription factor that plays a central role in the prevention of neoplastic transformation. Oligomerization appears to be essential for the tumor suppressing activity of p53 because oligomerization-deficient p53 mutants cannot suppress the growth of carcinoma cell lines. The crystal structure of the tetramerization domain of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and refined to a crystallographic R factor of 19.2 percent. The monomer, which consists of a β strand and an α helix, associates with a second monomer across an antiparallel β sheet and an antiparallel helix-helix interface to form a dimer. Two of these dimers associate across a second and distinct parallel helix-helix interface to form the tetramer.
Keywords
Antiparallel (mathematics)TetramerDimerAngstromCrystallographyChemistryHelix (gastropod)MonomerAlpha helixMutantProtein structureCrystal structureStereochemistryBiophysicsBiologyCircular dichroismBiochemistryGenePhysicsEnzyme
MeSH Terms
Computer GraphicsCrystallographyX-RayDNAHydrogen BondingMacromolecular SubstancesModelsMolecularProtein ConformationProtein StructureSecondaryTumor Suppressor Protein p53
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Publication Info
- Year
- 1995
- Type
- article
- Volume
- 267
- Issue
- 5203
- Pages
- 1498-1502
- Citations
- 543
- Access
- Closed
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Cite This
Philip D. Jeffrey,
Svetlana S. Gorina,
Nikola P. Pavletich
(1995).
Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms.
Science
, 267
(5203)
, 1498-1502.
https://doi.org/10.1126/science.7878469
Identifiers
- DOI
- 10.1126/science.7878469
- PMID
- 7878469