Year: 2016
Type: article
Abstract: The p53 tumor suppressor protein, whose mutation has been implicated in some half of all human cancers, adopts a homotetrameric quaternary structure as the biologically active form.While much is known about the monomeric structure of the DNA binding domain, two competing models of the complete tetramer differing in the relative orientation of the DNA binding interfaces prevail in the literature.In this study we investigate the plausibility of an alternate quaternary structure assembled by overlaying four copies of the full length monomer as completed by molecular modeling to the four fragments constituting the crystallized tetramerization domains.On the basis of this modeling we discuss the plausibility of an alternate quaternary structure of p53 as well as explore implications for the biological role of p53 as a major transcriptional regulator of the cell.
Source: MOJ Proteomics & Bioinformatics
Author: Kelly M Thayer
Institution: Skidmore College
Language: English
Subfield: Oncology
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
Funder: Vassar College
OpenAlex ID: W2463083996