Zusammenfassung
The cAMP-dependent protein kinase (PKA) and the cGMP-dependent protein kinase (PKG) are highly homologous enzymes differing in their specificity for cAMP and cGMP, respectively. Recent structure-function studies led to the identification of key residues responsible for cGMP-specificity in PKG. Introduction of these amino acids into PKA switches its cyclic nucleotide selectivity. Here we demonstrate that the same mutations turn a cAMP-specific FRET-based A-kinase activity reporter (AKAR) into a cGMP-specific reporter.
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