Sandbox SouthUniversity1: Difference between revisions
Arthur Cox (talk | contribs) No edit summary |
Arthur Cox (talk | contribs) No edit summary |
||
| Line 40: | Line 40: | ||
|| Feedback for distractor. | || Feedback for distractor. | ||
</quiz> | </quiz> | ||
The substrate (flavone) shown here is different from many other substrates of this CYP. Besides being a substrate of CYP1A2, it is also an inhibitor. It inhibits the metabolism of other CYP1A2 substrates because it binds very tightly to this enzyme. Thus, while the CYP is bound, it is unavailable to metabolize other substrates (e.g. drugs). Therefor, if a drug were to be coadministered with this compound, it would not be broken down to the extent expected, and could build up to toxic levels. | |||
The reason that this flavone is bound so tightly to the enzyme is that it's shape and electron density are complementary to the binding pocket. This is examined <scene name='Sandbox_SouthUniversity1/2hi4_blue_transparent_ribbons/1'>next.</scene> First examine the shape of the flavone bound to the protein. Next, the Van derWaals surface of the cavity is <scene name='Sandbox_SouthUniversity1/displayed./1'>TextToBeDisplayed</scene> | |||
Different members of the CYP450 enzymes preferentially metabolize different xenobiotics. What features of a drug do you think might cause it to be metabolized by one CYP versus another? | Different members of the CYP450 enzymes preferentially metabolize different xenobiotics. What features of a drug do you think might cause it to be metabolized by one CYP versus another? | ||
Draft: <illustration of residues in active site> | Draft: <illustration of residues in active site> | ||
Draft animation <scene name='Sandbox_SouthUniversity1/Act_residues_shown/1'>Highlighting residues around ligand</scene> | Draft animation <scene name='Sandbox_SouthUniversity1/Act_residues_shown/1'>Highlighting residues around ligand</scene> | ||