Figure 5.

Molecular modeling simulation of K114, SU 6656 and retinoic acid p-hydroxyanilide binding to the A₃AR. A side-on (A,C,E) and top-down (B,D,F) view of the top scoring binding poses for K114, SU 6656 and retinoic acid p-hydroxyanilide (dark gray liquorice coloring) respectively, bound into our previously reported A₃AR receptor homology model (Vernall et al., 2013). Previously identified amino acid side chain residues associated with the orthosteric binding pocket (Squarcialupi et al., 2013) are represented in light gray liquorice coloring and labeled alongside the TM loop regions for clarity.