Investigation by site-directed mutagenesis of the role of cytochrome P450 2B4 non-active-site residues in protein-ligand interactions based on crystal structures of the ligand-bound enzyme.

@article{Wilderman2012InvestigationBS,
  title={Investigation by site-directed mutagenesis of the role of cytochrome P450 2B4 non-active-site residues in protein-ligand interactions based on crystal structures of the ligand-bound enzyme.},
  author={P Ross Wilderman and Sean C Gay and Hyun-Hee Jang and Qinghai Zhang and Charles David Stout and James R. Halpert},
  journal={The FEBS journal},
  year={2012},
  volume={279 9},
  pages={
          1607-20
        }
}
Residues located outside the active site of cytochromes P450 2B have exhibited importance in ligand binding, structural stability and drug metabolism. However, contributions of non-active-site residues to the plasticity of these enzymes are not known. Thus, a systematic investigation was undertaken of unique residue-residue interactions found in crystal structures of P450 2B4 in complex with 4-(4-chlorophenyl)imidazole (4-CPI), a closed conformation, or in complex with bifonazole, an expanded… CONTINUE READING
BETA
1
Twitter Mention

Figures, Tables, and Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 16 CITATIONS

A structural snapshot of CYP2B4 in complex with paroxetine provides insights into ligand binding and clusters of conformational states.

  • The Journal of pharmacology and experimental therapeutics
  • 2013
VIEW 4 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

References

Publications referenced by this paper.
SHOWING 1-10 OF 65 REFERENCES

Features and development of Coot

  • Acta crystallographica. Section D, Biological crystallography
  • 2010

Polymorphic drug metabolism in anaesthe

JC Talakad, S Kumar, Halpert
  • Curr Drug Metab
  • 2009

Similar Papers

Loading similar papers…