Fig. 3: Structural comparison of NaVEhWT and NaVEhΔN.
From: Structural mechanism of voltage-gated sodium channel slow inactivation

a The superposition of NaVEhΔN and NaVEhWT (gray) viewed from the extracellular side (Left) and from the intracellular side (Right). The distances between neighboring subunits are labeled. b Conformational changes of NaVEhΔN (red) and NaVEhWT (gray). One subunit is shown in cartoon, and the other three are shown in half-transparent surface. The pore domains of two structures are superimposed. Red arrows indicate the conformational shifts. c The superposition of the VSDs of NaVEhΔN (red) and NaVEhWT (gray). S1-S3 are shown as cylindrical helices and S4 is shown as cartoon. Gating charge residues are shown as sticks. d The activation gate of NaVEhΔN (Left) and NaVEhWT (Right), respectively. The key hydrophobic residues are shown as sticks and spheres. e Selectivity filter comparison between NaVEhΔN and NaVEhWT. On the right, conformational changes of the P2 helix between NaVEhΔN and NaVEhWT. The red arrow indicates the conformational shift of P2 helix.