Article
Mutating protein kinase cAMP-binding sites into cGMP-binding sites. Mechanism of cGMP selectivity.
The Journal of biological chemistry - 25 Dec 1991
Shabb J B, Buzzeo B D, Ng L, Corbin J D
Abstract excerpt
The cAMP-dependent protein kinase contains two different cAMP-binding sites referred to as the slow and fast sites. Mutation of Ala-334 to a threonine in the slow site of the bovine type I regulatory subunit created a site with marked increase in cGMP affinity without changing cAMP affinity (Shabb, J. B., Ng. L., Corbin, J. D. (1990) J. Biol. Chem. 265, 16031-16034). The corresponding fast site residue (Ala-210)...
Topics
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites
- Cattle
- Cyclic AMP
- Cyclic GMP
- Enzyme Activation
- Molecular Sequence Data
- Mutation
- Protein Kinases
- Sequence Alignment
