Identification of residues crucially involved in soluble guanylate cyclase activation.

@article{Rothkegel2006IdentificationOR,
  title={Identification of residues crucially involved in soluble guanylate cyclase activation.},
  author={Christiane Rothkegel and Peter M Schmidt and Friederike Stoll and Henning Schr{\"o}der and Harald H. H. W. Schmidt and J. -P. Stasch},
  journal={FEBS letters},
  year={2006},
  volume={580 17},
  pages={4205-13}
}
The ubiquitous heterodimeric nitric oxide (NO) receptor soluble guanylate cyclase (sGC) plays a key role in various signal transduction pathways. Binding of NO takes place at the prosthetic heme moiety at the N-terminus of the beta(1)-subunit of sGC. The induced structural changes lead to an activation of the catalytic C-terminal domain of the enzyme and to an increased conversion of GTP into the second messenger cyclic GMP (cGMP). In the present work we selected and substituted different… CONTINUE READING