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

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.

SUBMITTER: Veglia G

PROVIDER: S-EPMC3821181 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature

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

Veglia Gianluigi G Cembran Alessandro A

The FEBS journal 20130827 22

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 kin ...[more]

PMID: 23902454

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