Introducing intrinsic disorder reduces electrostatic steering in protein-protein interactions.

ABSTRACT: Protein-protein interactions underlie many critical biology functions, such as cellular signaling and gene expression, in which electrostatic interactions can play a critical role in mediating the specificity and stability of protein complexes. A substantial portion of proteins are intrinsically disordered, and the influences of structural disorder on binding kinetics and thermodynamics have been widely investigated. However, whether the effect of electrostatic steering depends on structural disorder remains unexplored. In this work, we addressed the consequence of introducing intrinsic disorder in the electrostatic steering of the E3/Im3 complex using molecular dynamics simulation. Our results recapitulated the experimental observations that the responses of stability and kinetics to salt

SUBMITTER: Gao M 

PROVIDER: S-EPMC8390962 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature