Figure 4: Structural model of the NaV1.5 C-T.
From: Perturbation of sodium channel structure by an inherited Long QT Syndrome mutation
(a) Model of structured NaV1.5 C-T. The tryptophan (W1798) is shown as orange space-filling model. The H6 di-histidine pairs are indicated as in Figure 3 with Ni2+ ion coordinated by their respective di-histidine pairs shown as spheres of the same colour. The distances predicted by the model are 12.3, 15.2 and 14.1 Å for H6-N (blue), H6-M (red) and H6-C (green) di-histidines, respectively. (b) Interactions between side chains of residues on the N terminal end of H6 (H1900, V1903, S1904, V1907L denoted by yellow side chains) and side chains of residues on the H1–H2 linker (F1808, denoted by cyan side chain) and the H2–H3 linker (V1843 and S1844, also in cyan) as predicted by the model. (c) Interactions between side chains of residues at the C-T of H6 (R1914, H1915, Q1918 in yellow) and the aromatic residues on H1 (F1791 and Y1795, in cyan) also as predicted by the model.
