Chemical Physics Letters, Vol.730, 100-104, 2019
Exploring the autoinhibition mechanism of the C-terminal guanine nucleotide exchange factor module of Trio through molecular dynamics simulations
In this work, we carried out molecular dynamic simulations and hydrogen bonds analyses of the wild type TrioC and R2150A mutant respectively, and compared our results with the experimental observations. In either of the two systems, a stable hydrogen bonds network is formed near the DH-PH interface, contributing to maintaining the autoinhibited conformation of TrioC. Our work could be beneficial for the design of a small-molecule stabilizer of the autoinhibited TrioC conformation.