Electronic Polarization at the Interface between the p53 Transactivation Domain and Two Binding Partners.

ABSTRACT: Intrinsically disordered proteins (IDPs) are an abundant class of highly charged proteins that participate in numerous crucial biological processes, often in regulatory roles. IDPs do not have one major free energy minimum with a dominant structure, instead existing as conformational ensembles of multiple semistable conformations. p53 is a prototypical protein with disordered regions and binds to many structurally diverse partners, making it a useful model for exploring the role of electrostatic interactions at IDP binding interfaces. In this study, we used the Drude-2019 force field to simulate the p53 transactivation domain with two protein partners to probe the role of electrostatic interactions in IDP protein-protein interactions. We found that the Drude-2019 polarizable force field re

SUBMITTER: Corrigan AN 

PROVIDER: S-EPMC9267131 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature