Journal article
Change of Conformation of the DNA-binding Domain of p53 Is the Only Key Element for Binding of and Interference with p73*
Abstract
Xenopus p53 has biological and biochemical properties similar to those of human p53, except for optimal temperature. The frog protein is fully active at 30 degrees C and inactive at 37 degrees C, leading to a temperature-sensitive behavior similar to that of the human mutant p53Ala(143) and the murine mutant p53Val(135). Using hybrid proteins between human and Xenopus expressed from artificial p53 minigenes, we have been able to demonstrate …
Authors
Bensaad K; Le Bras M; Unsal K; Strano S; Blandino G; Tominaga O; Rouillard D; Soussi T
Journal
Journal of Biological Chemistry, Vol. 278, No. 12, pp. 10546–10555
Publisher
Elsevier
Publication Date
March 2003
DOI
10.1074/jbc.m208233200
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AnimalsApoptosisBinding SitesCells, CulturedDNADNA-Binding ProteinsGenes, Tumor SuppressorHumansNuclear ProteinsProtein ConformationRecombinant Fusion ProteinsStructure-Activity RelationshipTemperatureTranscription, GeneticTumor Protein p73Tumor Suppressor Protein p53Tumor Suppressor ProteinsXenopus