Skip to main content
. Author manuscript; available in PMC: 2009 Jun 1.
Published in final edited form as: Arch Biochem Biophys. 2008 Mar 25;474(1):198–204. doi: 10.1016/j.abb.2008.03.017

Figure 7.

Figure 7

Proposed model for Nile Red allosterism. Nile Red (maroon ellipse) binds with high affinity to the active site. Lower-affinity binding of a second Nile Red molecule at a peripheral effector binding site induces a conformational change that increases the accessibility of the active-site Nile Red molecule to the heme-iron center (red parallelogram). In contrast, effector molecules such as ANF (yellow) bind with higher affinity to the peripheral site, and can form a mixed ternary complex with CYP3A4 and Nile Red; the photophysical properties of Nile Red may provide insight into the nature of this mixed complex for different effectors.