Interaction of calmodulin with its binding domain of rat cerebellar nitric oxide synthase. A multinuclear NMR study.

@article{Zhang1995InteractionOC,
  title={Interaction of calmodulin with its binding domain of rat cerebellar nitric oxide synthase. A multinuclear NMR study.},
  author={Mingjie Zhang and Tao Yuan and James M. Aramini and Hans J. Vogel},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 36},
  pages={
          20901-7
        }
}
The intercellular messenger nitric oxide is produced through the action of nitric oxide synthases, a class of enzymes that is regulated by calcium-calmodulin (CaM). In this work, the interaction of CaM with a 23-amino-acid residue synthetic peptide, encompassing the CaM-binding domain of constitutive rat cerebellar nitric oxide synthase (cNOS), was investigated by various NMR methods. Cadmium-113 NMR studies showed that binding of the cNOS peptide increased the affinity of CaM for metal ions… CONTINUE READING

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