Stabilization of calmodulin-dependent protein kinase II through the autoinhibitory domain.

@article{Ishida1995StabilizationOC,
  title={Stabilization of calmodulin-dependent protein kinase II through the autoinhibitory domain.},
  author={A. Yoshihisa Ishida and Hitoshi Fujisawa},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 5},
  pages={2163-70}
}
The active 30-kDa chymotryptic fragment of calmodulin-dependent protein kinase II (CaM kinase II), devoid of the autoinhibitory domain, and the enzyme, autothiophosphorylated at Thr286/Thr287, were much more labile than was the original native enzyme. They were markedly stabilized by synthetic peptides, designed after the sequence around the autophosphorylation site in the autoinhibitory domain, such as autocamtide-2 and CaMK-(281-309), but such marked stabilizations were not observed with the… CONTINUE READING

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