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Conformational Equilibrium Of N-Myristoylated Camp-Dependent Protein Kinase A By Molecular Dynamics Simulations, Alessandro Cembran, Larry R. Masterson, Christopher L. Mcclendon, Susan S. Taylor, Jiali Gao, Gianluigi Veglia
Conformational Equilibrium Of N-Myristoylated Camp-Dependent Protein Kinase A By Molecular Dynamics Simulations, Alessandro Cembran, Larry R. Masterson, Christopher L. Mcclendon, Susan S. Taylor, Jiali Gao, Gianluigi Veglia
Larry Masterson
The catalytic subunit of protein kinase A (PKA-C) is subject to several post- or cotranslational modifications that regulate its activity both spatially and temporally. Among those, N-myristoylation increases the kinase affinity for membranes and might also be implicated in substrate recognition and allosteric regulation. Here, we investigated the effects of N-myristoylation on the structure, dynamics, and conformational equilibrium of PKA-C using atomistic molecular dynamics simulations. We found that the myristoyl group inserts into the hydrophobic pocket and leads to a tighter packing of the A-helix against the core of the enzyme. As a result, the conformational dynamics of the A-helix …