Influence of N-myristylation and ligand binding on the flexibility of the catalytic subunit of protein kinase A.

ABSTRACT: The catalytic (C) subunit of protein kinase A is regulated in part by cotranslational N-myristylation and ligand binding. Using a combination of time-resolved fluorescence anisotropy and molecular dynamics (MD) simulations, we characterized the effect of N-myristylation and ligand binding on C-subunit dynamics. Five single-site cysteine-substitution mutants of the C-subunit were engineered with and without N-terminal myristylation and labeled with fluorescein maleimide, and time-resolved fluorescence anisotropy decays were measured to assess the flexibility of the labeled regions in the presence and absence of ligands. A parallel set of in silico experiments were performed to complement the experimental findings. These experiments showed that myristylation produces both local and global ef

SUBMITTER: Bastidas AC 

PROVIDER: S-EPMC3788587 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature