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={Byung Je Sung and Kwang Yeon Hwang and Young Ho Jeon and Jae Il Lee and Yong-Seok Heo and Jin Hwan Kim and Jin Ho Moon and Jung-Min Yoon and Y L Hyun and Eunmi Kim and Sung Jin Eum and Sam-Yong Park and Jie-Oh Lee and Tae Gyu Lee and Seonggu Ro and Joong Myung 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… 

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