Implications of PDE4 structure on inhibitor selectivity across PDE families

@article{Ke2004ImplicationsOP,
  title={Implications of PDE4 structure on inhibitor selectivity across PDE families},
  author={Hengming Ke},
  journal={International Journal of Impotence Research},
  year={2004},
  volume={16},
  pages={S24-S27}
}
Phosphodiesterases (PDEs) control cellular concentrations of cyclic adenosine monophosphate (cAMP) or cyclic guanosine monophosphate (cGMP). PDE4 and PDE5 selectively hydrolyze cAMP and cGMP, respectively. PDE family members share approximately 25% sequence identity within a conserved catalytic domain of about 300 amino acids. Crystal structure analysis of PDE4's catalytic domain identifies two metal-binding sites: a high-affinity site and a low-affinity site, which probably bind zinc (Zn2… CONTINUE READING

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