Figure 6.
Structure of NaVAb/L101S. (A) Crystal structure of NaVAb/L101S with the mutation is shown in red. (B) Close-up view of NaVAb/L101S structure in the activated state (teal). Side chains of residues L101S (red), Arg99 (R1), and Arg102 (R2; cyan) are shown as sticks with the σA-weighted 2FO-FC electron density map contoured at 1.0σ level overlaid (mesh). A DMPC lipid molecule potentially interacting with L101S is shown as yellow sticks. The acyl chain of the DMPC is partially disordered. (C) Comparison of NaVAb/L101S structure (teal) with the structure of NaVAb WT (light orange). The DMPC molecule is fully ordered in the WT structure. NaVAbΔ28 (PDB accession no. 6MWA) was used for the comparison as WT. (D) Homology model of NaVAb/L101S structure in the resting state. DMPC lipid molecules are shown as yellow sticks to indicate the membrane bilayer. The L101S side chain is buried at the center of the membrane bilayer.

Structure of Na V Ab/L101S. (A) Crystal structure of NaVAb/L101S with the mutation is shown in red. (B) Close-up view of NaVAb/L101S structure in the activated state (teal). Side chains of residues L101S (red), Arg99 (R1), and Arg102 (R2; cyan) are shown as sticks with the σA-weighted 2FO-FC electron density map contoured at 1.0σ level overlaid (mesh). A DMPC lipid molecule potentially interacting with L101S is shown as yellow sticks. The acyl chain of the DMPC is partially disordered. (C) Comparison of NaVAb/L101S structure (teal) with the structure of NaVAb WT (light orange). The DMPC molecule is fully ordered in the WT structure. NaVAbΔ28 (PDB accession no. 6MWA) was used for the comparison as WT. (D) Homology model of NaVAb/L101S structure in the resting state. DMPC lipid molecules are shown as yellow sticks to indicate the membrane bilayer. The L101S side chain is buried at the center of the membrane bilayer.

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