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. Author manuscript; available in PMC: 2021 Jan 9.
Published in final edited form as: Cell. 2019 Dec 19;180(1):122–134.e10. doi: 10.1016/j.cell.2019.11.041

Figure 5. Activation and Fast Inactivation Gates.

Figure 5.

(A) Bottom view of the rNaV1.5C intracellular activation gate. The IFM motif (Ile1485-Phe1486-Met1487) and the sidechains of amino acid residues that partially close the activation gate are shown in sticks with half-transparent van der Waals surface.

(B) Close-up view of the rNaV1.5C intracellular activation gate aligned with the open-state structure of NavAb-Δ40 (PDB code: 5VB8) colored in magenta.

(C) Close-up view of the NaV1.5C intracellular activation gate aligned with the resting state model of rNaV1.5C activation gate calculated by MODELLER based on the resting state structure of NavAb (PDB code: 6P6W). The resting model is colored in orange with key residues sealing the activation gate shown in sticks and half-transparent van der Waals surface.

(D) Side view of the IFM motif shown in sticks with electron density mesh contoured at 3 σ.

(E) Close-up view of IFM motif bound to the hydrophobic pocket shown in yellow. Dotted line in red, hydrogen bond.

(F) Interaction of DIII-DIV linker with DIII and DIV S4-S5 linker. “(O)” indicates an important interaction with a backbone carbonyl group. Dotted line in red, hydrogen bond.

(G) Interaction of DIII S6 with DIII S4-S5 linker. “(O)” indicates an important interaction with a backbone carbonyl group. Dotted lines in red, hydrogen bonds.