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. 2017 Feb 1;8(6):401–438. doi: 10.1007/s13238-017-0372-z

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© The Author(s) 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Homology model structure of human Na_v1.7 sodium channel. (A) Intra-membrane view and extracellular view of the structure model of Na_v1.7. The four domains are colored green, light blue, cyan, and gray for domain I, II, III, and IV, respectively. (B) The pore domain of Na_v1.7 structure model. The S5–S6 segments of Na_v1.7 are shown and the four selectivity filter amino acids are shown as sticks (left). A close-up view of the four SF residues, D361 in domain I, E927 in domain II, K1406 in domain III, and A1698 in domain IV (right)