Part of the Advances in Experimental Medicine and Biology book series (volume 611)
Effects of Tumor-Associated Mutations in the p53 Tetramerization Domain on Oligomerization State and Transcriptional Activity
Tumor suppressor protein p53 plays an important role to maintain genomic integrity from cellular stress by trans-activating the target genes involved in different cellular functions, such as cell cycle arrest and apoptosis [ 1]. The tetramer formation of p53 through the C-terminal tetramerization domain (TD) is essential for its activity. The p53 tetramerization domain consists of a b-strand (Glu326-333), a tight turn (Gly334), and an α-helix (Arg335-Gly356) (Fig. 1A). Approximately 50 % of human tumors carry inactivating mutations in the p53 gene. To date, 41 point mutations have been found in 22 positions among 31 residues of the tetramerization domain (Fig. 1B). It is important to understand the mechanism of malignant transformation by mutations in the tetramerization domain [ 2, 3].
KeywordsHydrophobic Core Leu330 Residue Tetrameric Structure Mutant Peptide Tetramerization Domain
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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