Transcription factor p53, also known as tumor suppressor p53, is one of the most common mutated proteins found in cancer cells. p53 function is crucial for cell replication, DNA synthesis, and DNA repair, and it is a central target for the genetic diagnosis and therapy of cancer. In our project, 200 ns Molecular Dynamics (MD) simulations of 14 different p53 models and Root-Mean-Square Deviation (RMSD) calculations were used to study the system stability of the p53 dimer with or without DNA bound for the wildtype and various mutant forms of p53. From our MD movie analysis and RMSD calculations, the model of p53 binding with DNA shows that the integrity of the dimer interface is largely maintained throughout the MD simulations while most of the models without DNA bound show the dimer falling apart and rotating relative to one another by ~90°.

Computational analysis of the dimer interface of p53 bound to DNA

2019 Fall National Meeting

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