Identification of key amino acids in a conserved cGMP-binding site of cGMP-binding phosphodiesterases. A putative NKXnD motif for cGMP binding.

@article{Turko1996IdentificationOK,
  title={Identification of key amino acids in a conserved cGMP-binding site of cGMP-binding phosphodiesterases. A putative NKXnD motif for cGMP binding.},
  author={Illarion V Turko and Tamara L. Haik and Linda M. McAllister-Lucas and Frank Burns and Sharron H. Francis and Jackie D. Corbin},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 36},
  pages={22240-4}
}
cGMP-binding phosphodiesterases contain two kinetically distinct cGMP-binding sites (a and b), and each site contains a conserved N(K/R)XnFX3DE sequence. N276A, K277A, K277R, D289A, and E290A mutants in the N276KX7FX3DE290 sequence of site a (higher affinity site) of bovine cGMP-binding, cGMP-specific phosphodiesterase (cGB-PDE or PDE5A) were expressed in High Five cells and purified. The cGMP-binding affinities of three mutants [K277A (Kd approximately 12 microM), D289A (Kd approximately 24… CONTINUE READING