| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8291333 | Archives of Biochemistry and Biophysics | 2012 | 9 Pages |
Abstract
⺠We compared the interaction of CYP3A4 with the inhibitor ritonavir and two analogs. ⺠Peripheral binding of ritonavir limits and complicates the heme ligation kinetics. ⺠Active site residue Arg212 assists binding of ritonavir-like molecules to CYP3A4. ⺠CYP3A4-desthiazolylmethyloxycarbonyl ritonavir complex structure is determined. ⺠Structural data suggest how the inhibitory potency of ritonavir can be improved.
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Authors
Irina F. Sevrioukova, Thomas L. Poulos,