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1c26
From Proteopedia
| 1c26, resolution 1.70Å () | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
CRYSTAL STRUCTURE OF P53 TETRAMERIZATION DOMAIN
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.
Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms., Jeffrey PD, Gorina S, Pavletich NP, Science. 1995 Mar 10;267(5203):1498-502. PMID:7878469
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1c26 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Jeffrey PD, Gorina S, Pavletich NP. Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science. 1995 Mar 10;267(5203):1498-502. PMID:7878469
- Alibes A, Yankilevich P, Canada A, Diaz-Uriarte R. IDconverter and IDClight: conversion and annotation of gene and protein IDs. BMC Bioinformatics. 2007 Jan 10;8:9. PMID:17214880 doi:10.1186/1471-2105-8-9
