Calmodulin promotes dimerization of the oxygenase domain of human endothelial nitric-oxide synthase.

@article{Hellermann1997CalmodulinPD,
  title={Calmodulin promotes dimerization of the oxygenase domain of human endothelial nitric-oxide synthase.},
  author={Gary R. Hellermann and Larry P. Solomonson},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 18},
  pages={
          12030-4
        }
}
The active form of endothelial nitric-oxide synthase (eNOS) is a homodimer. The activity of the enzyme is regulated in vivo by calcium signaling involving the binding of calmodulin (CAM), which triggers the activation of eNOS. We have examined the possible role of calcium-mediated CAM binding in promoting dimerization of eNOS through the oxygenase domain of the enzyme. A recombinant form of the oxygenase domain of human eNOS was expressed in a prokaryotic expression system. This recombinant… CONTINUE READING
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