Mechanism of PhosphoThreonine/Serine Recognition and Specificity for Modular Domains from All-atom Molecular Dynamics.

ABSTRACT:

Background

Phosphopeptide-binding domains mediate many vital cellular processes such as signal transduction and protein recognition. We studied three well-known domains important for signal transduction: BRCT repeats, WW domain and forkhead-associated (FHA) domain. The first two recognize both phosphothreonine (pThr) and phosphoserine (pSer) residues, but FHA has high specificity for pThr residues. Here we used molecular dynamics (MD) simulations to reveal how FHA exclusively chooses pThr and how BRCT and WW recognize both pThr/pSer. The work also investigated the energies and thermodynamic information of intermolecular interactions.

Results

Simulations carried out included wide-type and mutated systems. Through analysis of MD simulations, we found that the conserved His res

SUBMITTER: Huang YM 

PROVIDER: S-EPMC3146460 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature