Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat

@article{Pemble2007CrystalSO,
  title={Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat},
  author={Charles W Pemble and Lynnette C. Johnson and Steven J. Kridel and W. Todd Lowther},
  journal={Nature Structural \&Molecular Biology},
  year={2007},
  volume={14},
  pages={704-709}
}
Human fatty acid synthase (FAS) is uniquely expressed at high levels in many tumor types. Pharmacological inhibition of FAS therefore represents an important therapeutic opportunity. The drug Orlistat, which has been approved by the US Food and Drug Administration, inhibits FAS, induces tumor cell–specific apoptosis and inhibits the growth of prostate tumor xenografts. We determined the 2.3-Å-resolution crystal structure of the thioesterase domain of FAS inhibited by Orlistat. Orlistat was… 
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