Crystal structure of phosphodiesterase 9 shows orientation variation of inhibitor 3-isobutyl-1-methylxanthine binding.

@article{Huai2004CrystalSO,
  title={Crystal structure of phosphodiesterase 9 shows orientation variation of inhibitor 3-isobutyl-1-methylxanthine binding.},
  author={Qing Wang Huai and Huanchen Wang and Wei Zhang and Robert W. Colman and Howard Robinson and Hengming Ke},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 26},
  pages={9624-9}
}
Cyclic nucleotide phosphodiesterases (PDEs) are enzymes controlling cellular concentrations of the second messengers cAMP and cGMP. The crystal structure of the catalytic domain of PDE9A2, a member of a PDE family specifically hydrolyzing cGMP, has been determined at 2.23-A resolution. The PDE9A2 catalytic domain closely resembles the cAMP-specific PDE4D2 but is significantly different from the cGMP-specific PDE5A1, implying that each individual PDE family has its own characteristic substrate… CONTINUE READING