Article
Restoration of the calcium binding activity of mutant calmodulins toward normal by the presence of a calmodulin binding structure.
The Journal of biological chemistry - 25 Feb 1991
Haiech J, Kilhoffer M C, Lukas T J, Craig T A, Roberts D M, Watterson D M
Abstract excerpt
The altered calcium binding activity of calmodulins (CaM) with point mutations can be restored toward that of wild type CaMs by the formation of a complex between CaM and a CaM binding sequence. Three different site-specific mutations resulted in selective effects on the apparent stoichiometry and affinity of CaM for calcium, with maintenance of the ability to activate myosin light chain kinase. The effects on...
Topics
- Amino Acid Sequence
- Binding Sites
- Calcium
- Calmodulin
- Enzyme Activation
- Molecular Sequence Data
- Mutation
- Myosin-Light-Chain Kinase