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. Author manuscript; available in PMC: 2020 Aug 8.
Published in final edited form as: Cell. 2019 Jul 25;178(4):993–1003.e12. doi: 10.1016/j.cell.2019.06.031

Figure 6. Gating Mechanism for Voltage-gated Sodium Channels.

Figure 6

(A) Superposition of structures of NaVAb in the resting/closed state and the activated/open state (PDB 5VB8) viewed from the intracellular side. Major structural changes are observed in the S4-S5 linker, and the S6 activation gate (red for the resting/closed state vs. green for the activated/open state).

(B) Interactions between the S4-S5 linker and S6 near the activation gate. The elbow movement of the S4-S5 linker from the resting/closed state (left) to the activated/open state (right) causes an exchange in the interactions between the S4-S5 linker residues (blue) and the S6 residues (red for the resting/closed state vs. green for the activated/open state) surrounding the activation gate of the pore.

(C) Solvent accessibility surface of NaVAb in the resting closed state (left) and the activated/open state (right). The pore is tightly closed at the activation gate in the resting state (red) but wide open in the activated open state (green).

(D) Structural transition between resting and activated states. Images of structures in the resting (left), intermediate (middle), and activated/open states (right) are captured from Video S1 and rendered as in Figure 5. Part of S3 is omitted for clarity.

See also Video S2.