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. 2016 Oct 31;7(4):60. doi: 10.3390/insects7040060

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© 2016 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).

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The pore-domain model of the mosquito sodium channel. (A, B), Side views; (C) Extracellular view; (D) Intracellular view. Helical segments of the channel protein in domains I, II, III, and IV are shown as yellow, red, green, and gray cylinders, respectively. Location of the pyrethroid receptor sites PyR1 and PyR2 is indicated by the magenta and blue circles, respectively. The four positions where three kdr mutations are detected in the mosquito sodium channel and another kdr mutation (L1014F) in other insect sodium channels are shown as space-filled side chains of the wild-type residues. Only carbon atoms (gray spheres) in these side chains are shown, whereas the hydrogen atoms are removed for clarity. Note that opposite faces of helix IIS6 contain residues that contribute to PyR1 (V1016) or PyR2 (I1011 and L1014).

The pore-domain model of the mosquito sodium channel. (A, B), Side views; (C) Extracellular view; (D) Intracellular view. Helical segments of the channel protein in domains I, II, III, and IV are shown as yellow, red, green, and gray cylinders, respectively. Location of the pyrethroid receptor sites PyR1 and PyR2 is indicated by the magenta and blue circles, respectively. The four positions where three kdr mutations are detected in the mosquito sodium channel and another kdr mutation (L1014F) in other insect sodium channels are shown as space-filled side chains of the wild-type residues. Only carbon atoms (gray spheres) in these side chains are shown, whereas the hydrogen atoms are removed for clarity. Note that opposite faces of helix IIS6 contain residues that contribute to PyR1 (V1016) or PyR2 (I1011 and L1014).