A Computational Approach for the Prediction of p53 and BCL-2 Protein-Protein Interactions.

ABSTRACT: p53 has long been studied as a major regulator in cellular pathways, resulting in a plethora of information on the structure and function of this protein as a frequently mutated tumor suppressor. Recent studies have demonstrated how the p53 transcription activation domain (TAD) interacts with the BH3-binding pocket of BCL-2 to regulate cell survival/death. While the in vitro studies on p53 and BCL-2 have frequently used truncated and stabilized proteins of p53 to ensure crystallization, these mutated proteins are not naturally observed in cells. Thus, it becomes important to find a way in silico to simulate how a full-length monomer with the unaltered sequence of wild-type (WT) or missense mutant (MT) p53 interacts with BCL-2. Our objective is to provide a predictive insight into how p53 m

SUBMITTER: Creamer C 

PROVIDER: S-EPMC12785448 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature