Long-range molecular dynamics show that inactive forms of Protein Kinase A are more dynamic than active forms.

ABSTRACT: Many protein kinases are characterized by at least two structural forms corresponding to the highest level of activity (active) and low or no activity, (inactive). Further, protein dynamics is an important consideration in understanding the molecular and mechanistic basis of enzyme function. In this work, we use protein kinase A (PKA) as the model system and perform microsecond range molecular dynamics (MD) simulations on six variants which differ from one another in terms of active and inactive form, with or without bound ligands, C-terminal tail and phosphorylation at the activation loop. We find that the root mean square fluctuations in the MD simulations are generally higher for the inactive forms than the active forms. This difference is statistically significant. The higher dynamics

SUBMITTER: Kalaivani R 

PROVIDER: S-EPMC6371217 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature