Computational Investigation on the p53–MDM2 Interaction Using the Potential of Mean Force Study
Pundarikaksha Das, Venkata Satish Kumar Mattaparthi
Abstract
). The p53-MDM2 complex binding profile was observed to follow the same trend even in the duplicate simulation run and also in the simulation carried out with different force fields. We found that Lys51, Leu54, Tyr100, and Tyr104 from MDM2 and the residues Phe19, Trp23, and Leu26 from p53 provide the highest energy contributions for the p53-MDM2 interaction. Our findings highlight the prominent structural and binding characteristics of the p53-MDM2 complex that may be useful in designing potential inhibitors to disrupt the p53-MDM2 interactions.
Topics & Concepts
TransactivationMdm2Salt bridgeMolecular dynamicsDissociation (chemistry)Umbrella samplingChemistryBiophysicsSmall moleculeMoleculeMaterials scienceComputational chemistryBiologyBiochemistryMutantApoptosisPhysical chemistryGeneOrganic chemistryTranscription factorCancer-related Molecular PathwaysEnzyme Structure and FunctionDNA and Nucleic Acid Chemistry