The role of the αC-β4 loop in regulating cooperativity interaction in Protein Kinase A

This investigation examines the cooperative modulation of Protein Kinase A (PKA) activity by ATP and substrates, with a specialized focus on the enzyme's catalytic subunit (PKA-C), utilizing NMR-restrained molecular dynamics simulations complemented by advanced Markov Model analysis. Herein, we deposit chemical shift datasets for the PKA-C mutant F100A, both in its apo form and in complex with nucleotides and inhibitors, and activity assay data providing a comprehensive insight into the enzyme's allosteric regulation mechanisms.