Proteolytic cleavage sites in smooth muscle myosin-light-chain kinase and their relation to structural and regulatory domains.

@article{Pearson1991ProteolyticCS,
  title={Proteolytic cleavage sites in smooth muscle myosin-light-chain kinase and their relation to structural and regulatory domains.},
  author={Richard B Pearson and Makoto Ito and Nicholas A. Morrice and Anne K. Smith and Rosemary Condron and Richard E. H. Wettenhall and Bruce E. Kemp and David J. Hartshorne},
  journal={European journal of biochemistry},
  year={1991},
  volume={200 3},
  pages={723-30}
}
Proteolysis of the smooth muscle myosin-light-chain kinase with either thermolysin or endoproteinase Lys-C cleaves the enzyme towards the amino-terminus between the first and second unc domains, unc-II-1 and unc-II-2, and in the calmodulin-binding domain. The thermolytic fragment extends 532 residues from Ser275 to Ala806 and is resistant to further… CONTINUE READING