Folding and activity of cAMP-dependent protein kinase mutants.

doi:10.1016/j.febslet.2005.06.015

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Article

Folding and activity of cAMP-dependent protein kinase mutants.

FEBS letters - 1 Aug 2005

Langer Thomas, Sreeramulu Sridhar, Vogtherr Martin, Elshorst Bettina, Betz Marco, Schieborr Ulrich, Saxena Krishna, Schwalbe Harald

Abstract excerpt

The catalytic subunit of cAMP-dependent protein kinase (PKA) can easily be expressed in Escherichia coli and is catalytically active. Four phosphorylation sites are known in PKA (S10, S139, T197 and S338), and the isolated recombinant protein is a mixture of different phosphorylated forms. Obtaining uniformly phosphorylated protein requires separation of the protein preparation leading to significant loss in...

Topics

Cyclic AMP-Dependent Protein Kinases
Escherichia coli
Models, Molecular
Mutation
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Protein Folding
Recombinant Proteins

Source

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Identifiers

PMID: 16026785
DOI: 10.1016/j.febslet.2005.06.015

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