1C26

CRYSTAL STRUCTURE OF P53 TETRAMERIZATION DOMAIN

Summary for 1C26

• Entry DOI: 10.2210/pdb1c26/pdb
• Descriptor: P53 TUMOR SUPPRESSOR (2 entities in total)
• Functional Keywords: tetramer, gene regulation
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637
• Total number of polymer chains: 1
• Total formula weight: 3823.27

Authors

Jeffrey, P.D.,Gorina, S.,Pavletich, N.P. (deposition date: 1999-07-22, release date: 1999-07-27, Last modification date: 2024-02-07)

Primary citation

Jeffrey, P.D.,Gorina, S.,Pavletich, N.P.
Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms.
Science, 267:1498-1502, 1995

PubMed 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.

PubMed: 7878469

Experimental method

X-RAY DIFFRACTION (1.7 Å)