Conformational diversity and ligand tunnels of mammalian cytochrome P450s.

@article{Yu2013ConformationalDA,
  title={Conformational diversity and ligand tunnels of mammalian cytochrome P450s.},
  author={Xiaofeng Yu and Vlad Cojocaru and Rebecca C. Wade},
  journal={Biotechnology and applied biochemistry},
  year={2013},
  volume={60 1},
  pages={134-45}
}
The mammalian cytochrome P450 (CYP) enzymes play important roles in drug metabolism, steroid biosynthesis, and xenobiotic degradation. The active site of CYPs is buried in the protein and thus the ligands have to enter and exit the active site via ligand tunnels. Conformational changes of flexible parts of the protein usually accompany the entrance and exit of ligands. Comparison of the crystal structures of mammalian CYPs in closed, open, and partially open states reveals that the greatest… CONTINUE READING
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Cytochrome P450: Structure, Mechanism, and Biochemistry (Ortiz de Montellano, P

  • T. L. Poulos, J. Cupp-Vickery, H. Li
  • 1995
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