Abstract
Protein kinase A (PKA) is the archetypical phosphokinase, sharing a catalytic core with the entire protein kinase superfamily. In eukaryotes, the ubiquitous location of PKA makes it one of the most important cellular signaling molecules, involved in a myriad of events. The catalytic subunit of PKA (PKA-C) is one of the most studied enzymes and was the first kinase to be crystallized; however, the effects of ligand binding, post-translational modifications and mutations on the activity of the kinase have been difficult to understand with only structural data. Here, we review our latest NMR studies on PKA-C, the results of which underscore the role of fast and slow conformational dynamics in the activation and inhibition of the kinase. Here, we review our latest NMR studies on the C subunit of the protein kinase A, underscoring the role of fast and slow conformational dynamics in both the activation and inhibition of the kinase.
Original language | English (US) |
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Pages (from-to) | 5608-5615 |
Number of pages | 8 |
Journal | FEBS Journal |
Volume | 280 |
Issue number | 22 |
DOIs | |
State | Published - Nov 2013 |
Keywords
- NMR relaxation
- allostery
- catalysis
- conformational entropy
- conformational selection
- phospholamban
- phosphorylation
- protein kinase A
- structural dynamics
- substrate recognition