Structural basis of the intrasteric regulation of myosin light chain kinases.

@article{Knighton1992StructuralBO,
  title={Structural basis of the intrasteric regulation of myosin light chain kinases.},
  author={Daniel R. Knighton and Richard B Pearson and Janusz M. Sowadski and Anthony R. Means and Lynn F Ten Eyck and Susan S. Taylor and Bruce E. Kemp},
  journal={Science},
  year={1992},
  volume={258 5079},
  pages={130-5}
}
The smooth muscle myosin light chain kinase (smMLCK) catalytic core was modeled by using the crystallographic coordinates of the cyclic AMP-dependent protein kinase catalytic subunit (cAPK) and a bound pseudosubstrate inhibitor peptide, PKI(5-24). Despite only 30% identity in amino acid sequence, the MLCK sequence can be readily accommodated in this structure. With the exception of the short B-helix, all major elements of secondary structure in the core are very likely conserved. The active… CONTINUE READING

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