The p53 tetramer shows an induced-fit interaction of the C-terminal domain with the DNA-binding domain.

ABSTRACT: The Trp53 gene is the most frequently mutated gene in all human cancers. Its protein product p53 is a very powerful transcription factor that can activate different biochemical pathways and affect the regulation of metabolism, senescence, DNA damage response, cell cycle and cell death. The understanding of its function at the molecular level could be of pivotal relevance for therapy. Investigation of long-range intra- and interdomain communications in the p53 tetramer-DNA complex was performed by means of an atomistic model that included the tetramerization helices in the C-terminal domain, the DNA-binding domains and a consensus DNA-binding site of 18 base pairs. Nonsymmetric dynamics are illustrated in the four DNA-binding domains, with loop L1 switching from inward to outward conformati

SUBMITTER: D'Abramo M 

PROVIDER: S-EPMC4929483 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature