Molecular dynamics simulation of phosphorylated KID post-translational modification.

ABSTRACT:

Background

Kinase-inducible domain (KID) as transcriptional activator can stimulate target gene expression in signal transduction by associating with KID interacting domain (KIX). NMR spectra suggest that apo-KID is an unstructured protein. After post-translational modification by phosphorylation, KID undergoes a transition from disordered to well folded protein upon binding to KIX. However, the mechanism of folding coupled to binding is poorly understood.

Methodology

To get an insight into the mechanism, we have performed ten trajectories of explicit-solvent molecular dynamics (MD) for both bound and apo phosphorylated KID (pKID). Ten MD simulations are sufficient to capture the average properties in the protein folding and unfolding.

Conclusions

Room-temperature MD

SUBMITTER: Chen HF 

PROVIDER: S-EPMC2717803 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature