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J. Biol. Chem., Vol. 265, Issue 27, 16031-16034, Sep, 1990
JB Shabb, L Ng and JD Corbin
Discrimination between cAMP and cGMP is a critical feature of cAMP- and
cGMP-dependent protein kinases. An alanine/threonine difference in the
cyclic nucleotide-binding sites has been proposed to provide a structural
basis for this functional distinction. Site-directed mutagenesis of this
alanine to a threonine in a cAMP-binding site of cAMP kinase produced a
mutant with markedly increased cGMP affinity as determined by cGMP binding
and protein kinase activation assays. Studies of other mutants at this
position support the role of the threonine hydroxyl group as the component
that enhances cGMP binding affinity.
One amino acid change produces a high affinity cGMP-binding site in cAMP-dependent protein kinase
Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
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