Figure 8

Structural model and docking poses AmNa_V1.

(a) Top view of one of the poses used for the docking calculations. The protein is in grey with the exception of the first domain, which is in blue. The residues involved in the binding site mapped by Du et al. in the A. aegypti channel are in purple. (b) A close-up view of the pore from the top, with the most populated docking pose for TTX. The most populated docking pose for TTX is in orange. The α-carbon of the residues involved in the DEKA motif of the selectivity filter are in green (D386, E989, K1496 and A1789). The residues located within 4.5 Å of the toxin which are known to contribute to TTX binding in mammalian sodium channels are displayed in yellow (Y387, W388, E389, G988, G1497 and D1792). The α-carbon of other residues known to contribute to TTX binding in mammalian sodium channels according to the model published by Tikhonov and Zhorov but not located within 4.5 Å of the TTX cluster are displayed in red (W990, E992, W1498, Q1500 and W1791). The α-carbon of the residues located within 4.5 Å of the TTX cluster but not considered to play a major role in TTX binding according to Tikhonov and Zhorov are shown in orange (D386, Y387, E389 E989, K1496, A1789 and D1792). (c) The most populated docking poses for permethrin are shown on a side view of the protein. (d) The most populated docking poses for fenvalerate are shown in the same view. The residues in purple in c and d are the residues involved in the binding site mapped by Du et al.