Role of conformational entropy in the activity and regulation of the catalytic subunit of protein kinase A

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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 languageEnglish (US)
Pages (from-to)5608-5615
Number of pages8
JournalFEBS Journal
Volume280
Issue number22
DOIs
StatePublished - Nov 2013

Keywords

  • NMR relaxation
  • allostery
  • catalysis
  • conformational entropy
  • conformational selection
  • phospholamban
  • phosphorylation
  • protein kinase A
  • structural dynamics
  • substrate recognition

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