Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms
- 10 March 1995
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 267 (5203) , 1498-1502
- https://doi.org/10.1126/science.7878469
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 beta strand and an alpha helix, associates with a second monomer across an antiparallel beta 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
This publication has 40 references indexed in Scilit:
- Mediation of c-Myc-Induced Apoptosis by p53Science, 1994
- High-Resolution Structure of the Oligomerization Domain of p53 by Multidimensional NMRScience, 1994
- Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic MutationsScience, 1994
- Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein.Genes & Development, 1994
- Altered cell cycle arrest and gene amplification potential accompany loss of wild-type p53Published by Elsevier ,1992
- Wild-type p53 restores cell cycle control and inhibits gene amplification in cells with mutant p53 allelesCell, 1992
- The p53 tumour suppressor geneNature, 1991
- Different Tumor-Derived p53 Mutants Exhibit Distinct Biological ActivitiesScience, 1990
- Structure of the ColE1 Rop protein at 1.7 Å resolutionJournal of Molecular Biology, 1987
- Resolution of time-of-flight small-angle neutron diffractometersJournal of Applied Crystallography, 1987