Effects of Myosin Light Chain Kinase and Peptides on Ca2+ Exchange with the N- and C-terminal Ca2+ Binding Sites of Calmodulin (*)

@article{Johnson1996EffectsOM,
  title={Effects of Myosin Light Chain Kinase and Peptides on Ca2+ Exchange with the N- and C-terminal Ca2+ Binding Sites of Calmodulin (*)},
  author={J. David Johnson and Christopher H. Snyder and M Walsh and M Flynn},
  journal={The Journal of Biological Chemistry},
  year={1996},
  volume={271},
  pages={761 - 767}
}
Myosin light chain kinase and peptides from the calmodulin (CaM) binding domains of myosin light chain kinase (RS-20, M-13), CaM kinase II, and the myristoylated alanine-rich protein kinase C substrate protein slowed Ca2+ dissociation from CaM's N-terminal sites from 405 ± 75/s to 1.8-2.9/s and from CaM's C-terminal sites from 2.4 ± 0.2/s to 0.1-0.4/s at 10°C. Since Ca2+ dissociates 5-29 times faster from the N-terminal in these CaM·peptide complexes and both lobes are required for activation… Expand
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