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. Author manuscript; available in PMC: 2020 Dec 1.
Published in final edited form as: Nat Chem Biol. 2020 Nov 16;16(12):1314–1320. doi: 10.1038/s41589-020-0644-4

Figure 4. Mammalian NaV and bacterial NaVAb are structurally conserved.

Figure 4.

a-b, Superposition between rat NaV1.5 (light gray) and NaVAb (blue) from side view (a) and bottom view (b). The fast inactivation gate and its key Isoleucine-Phenylalanine-Methionine (IFM) motif are highlighted in purple. c-d, Superposition of the selectivity filter of NaV1.5 domains I and III (c), and domains II and IV (d) with the selectivity filter of NaVAb from side view. e, Key specialized and conserved side chains at the selectivity filter viewed from extracellular side. NaV1.5 uses specific “DEKA” side chains while NaVAb uses four glutamates to partially dehydrate and conduct sodium ions. f-g, Superposition of the activation gate of NaV1.5 domains I and III (f), and domains II and IV (g) with the activation gate of NaVAb from side view. h, Key specialized side chains in NaV1.5 and NaVAb that modulate the shape and diameter of the activation gate.