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Science 10 March 1995:
Vol. 267. no. 5203, pp. 1498 - 1502
DOI: 10.1126/science.7878469

Articles

Science, Vol 267, Issue 5203, 1498-1502
Copyright © 1995 by American Association for the Advancement of Science


articles

Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms

PD Jeffrey, S Gorina, and NP Pavletich

Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.

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.


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HSP70 Binding Sites in the Tumor Suppressor Protein p53.
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Transcription of the Acanthamoeba TATA-binding Protein Gene. A SINGLE TRANSCRIPTION FACTOR ACTS BOTH AS AN ACTIVATOR AND A REPRESSOR.
W. Huang and E. Bateman (1997)
J. Biol. Chem. 272, 3852-3859
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p53: puzzle and paradigm..
L J Ko and C Prives (1996)
Genes & Dev. 10, 1054-1072
   PDF »
Interhelical angles in the solution structure of the oligomerization domain of p53: correction.
G. Clore, J. Omichinski, K Sakaguchi, N Zambrano, H Sakamoto, E Appella, and A. Gronenborn (1995)
Science 267, 1515-1516
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p53 Amino Acids 339-346 Represent the Minimal p53 Repression Domain.
T.-M. Hong, J. J. W. Chen, K. Peck, P.-C. Yang, and C.-W. Wu (2001)
J. Biol. Chem. 276, 1510-1515
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Crystal Structure of the Mouse p53 Core DNA-binding Domain at 2.7 A Resolution.
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   Abstract »    Full Text »    PDF »
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X.-T. Kong, H. Gao, and E. J. Stanbridge (2001)
J. Biol. Chem. 276, 32990-33000
   Abstract »    Full Text »    PDF »
High Thermostability and Lack of Cooperative DNA Binding Distinguish the p63 Core Domain from the Homologous Tumor Suppressor p53.
C. Klein, G. Georges, K.-P. Kunkele, R. Huber, R. A. Engh, and S. Hansen (2001)
J. Biol. Chem. 276, 37390-37401
   Abstract »    Full Text »    PDF »
Transcriptional Repression of the Anti-apoptotic survivin Gene by Wild Type p53.
W. H. Hoffman, S. Biade, J. T. Zilfou, J. Chen, and M. Murphy (2002)
J. Biol. Chem. 277, 3247-3257
   Abstract »    Full Text »    PDF »
NMR Spectroscopy Reveals the Solution Dimerization Interface of p53 Core Domains Bound to Their Consensus DNA.
C. Klein, E. Planker, T. Diercks, H. Kessler, K.-P. Kunkele, K. Lang, S. Hansen, and M. Schwaiger (2001)
J. Biol. Chem. 276, 49020-49027
   Abstract »    Full Text »    PDF »



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