The constructed model is consistent with the dimeric
mode observed in the crystal structures of other ABC transporters. To verify our structural model, an ATP
substrate was docked into the nucleotide-binding site. The predicted binding mode shows consistency
with related crystallographic findings and CFTR functional studies. Finally, genistein, an agent that
enhances CFTR activity, though the mechanism for such enhancement is unclear, was docked to the
model. Our predictions agreed with genistein’s bell-shaped dose–response relationship. Potential
mutagenesis experiments were proposed for understanding the potentiation mechanism of genistein
and for providing insightful information for drug design targeting at CFTR. The method used in this study
can be applied to modeling studies of other dimeric protein structures