Studies on Regioselective Binding Mode of Steroid Molecules in Homology Modeled Cytochrome P450-2C11 Academic Article uri icon


  • AbstractIn this study, we investigated the regioselective binding mode of steroid molecules and structure requirements for steroid molecules for 16[alpha]-hydroxylation by Cytochrome P450-2C11. Docking study by using the homology Cytochrome P450-2C11 indicated that 16[alpha]-hydroxylation is favored with steroidal molecules possessing the following components, 1) a bent A-B ring configuration (5[beta]-reduced), 2) C-3[alpha]-hydroxyl group, 3) C-17[beta]-acetyl group, and 4) methyl group at both the C-18 and C-19. These respective steroid components requirements such as A-B ring configuration and functional groups at C-3 and C-17 were defined as the inhibitory contribution factor. Overall results by rat CYP2C11 revealed that steroidal structure requirements resulted in causing an effective inhibition of [^3^H]progesterone 16[alpha]-hydroxylation by the adult male rat liver microsome. As far as docking of homology modeled CYP2C11 against investigated steroids is concerned, they are docked at the active site superimposed with flurbiprofen. It was also found that the distance between heme iron and C16[alpha]-H was between 4 to 6 and that the related angle was in the range of 18045.

published proceedings

  • Nature Precedings

author list (cited authors)

  • Ali, H., Yamada, M., Fujita, H., & Akaho, E.

citation count

  • 0

complete list of authors

  • Ali, Hamed||Yamada, Morio||Fujita, Hukihisa||Akaho, Eiichi

publication date

  • 2009