Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules

@article{Sung2003StructureOT,
  title={Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules},
  author={B. Sung and K. Hwang and Y. Jeon and J. I. Lee and Y. Heo and J. H. Kim and J. Moon and J. M. Yoon and Y. Hyun and Eunmi Kim and S. Eum and Sam-Yong Park and Jie-Oh Lee and Tae Gyu Lee and S. Ro and J. Cho},
  journal={Nature},
  year={2003},
  volume={425},
  pages={98-102}
}
Phosphodiesterases (PDEs) are a superfamily of enzymes that degrade the intracellular second messengers cyclic AMP and cyclic GMP. As essential regulators of cyclic nucleotide signalling with diverse physiological functions, PDEs are drug targets for the treatment of various diseases, including heart failure, depression, asthma, inflammation and erectile dysfunction. Of the 12 PDE gene families, cGMP-specific PDE5 carries out the principal cGMP-hydrolysing activity in human corpus cavernosum… Expand
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