Wang, Y.; Kim, J.; Olivieri, C.; Gao, J.; Veglia, G. Biophysical Journal, 2018, 114(3), 190a.
Eukaryotic protein kinases (EPK) serve as on-and-off switches for regulating various signaling cascades. Their aberrant activation is implicated in various human diseases such as cancer and heart failure. Unlike many other members in the EPK family, the catalytic subunit of protein kinase A (PKA-C) is constitutively active. Recent NMR relaxation dispersion experiment, however, suggest that sparsely-populated, conformationally excited states in PKA-C exist, revealing an equilibrium between different conformations in the μs to ms timescale.