X-ray crystal structure and binding mode analysis of human S-adenosylhomocysteine hydrolase complexed with novel mechanism-based inhibitors, haloneplanocin A analogues.

@article{Lee2011XrayCS,
  title={X-ray crystal structure and binding mode analysis of human S-adenosylhomocysteine hydrolase complexed with novel mechanism-based inhibitors, haloneplanocin A analogues.},
  author={Kang Man Lee and Won Jun Choi and Yoonji Lee and Hyun Joo Lee and Long Xuan Zhao and Hyuk Woo Lee and Jae Gyu Park and Hea O K Kim and Kwang Yeon Hwang and Yong-Seok Heo and Sun Choi and Lak Shin Jeong},
  journal={Journal of medicinal chemistry},
  year={2011},
  volume={54 4},
  pages={
          930-8
        }
}
The X-ray crystal structure of human S-adenosylhomocysteine (AdoHcy) hydrolase was first determined as a tetrameric form bound with the novel mechanism-based inhibitor fluoroneplanocin A (4b). The crystallized enzyme complex showed the closed conformation and turned out to be the intermediate of mechanism-based inhibition. It confirmed that the cofactor depletion by 3'-oxidation of fluoroneplanocin A contributes to the enzyme inhibition along with the irreversible covalent modification of… CONTINUE READING
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