An open conformation of mammalian cytochrome P450 2B4 at 1.6-A resolution.

@article{Scott2003AnOC,
  title={An open conformation of mammalian cytochrome P450 2B4 at 1.6-A resolution.},
  author={Emily E Scott and You Ai He and Michael R. Wester and Mark A White and Christopher C Q Chin and James R. Halpert and Eric F Johnson and Charles David Stout},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 23},
  pages={13196-201}
}
The xenobiotic metabolizing cytochromes P450 (P450s) are among the most versatile biological catalysts known, but knowledge of the structural basis for their broad substrate specificity has been limited. P450 2B4 has been frequently used as an experimental model for biochemical and biophysical studies of these membrane proteins. A 1.6-A crystal structure of P450 2B4 reveals a large open cleft that extends from the protein surface directly to the heme iron between the alpha-helical and beta… CONTINUE READING

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Molecular modeling of mammalian cytochrome P450s.

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Methods Enzymol

E. A. Merritt, D. J. Bacon
PNAS November • 1997

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