Figure 5.
Structure of NaVAb/L98R. (A) Crystal structure of NaVAb/L98R with the mutation shown in red. (B) Close-up view of NaVAb/L98R structure in the activated state (teal). Side chains of residues L98R (red), Glu32, 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). The S3–S4 loop and the side chain of L98R are disordered. (C) Comparison of NaVAb/L98R structure (teal) with the structure of NaVAb WT (light orange). A hypothetical model for the L98R side chain (red) is illustrated to indicate a favorable rotamer that does not clash with the S3–S4 loop. NaVAb/I217C (PDB accession no. 3RVY) was used for the comparison as WT because the S3–S4 loop was not modeled in NaVAbΔ28 (PDB accession no. 6MWA). (D) Homology model of NaVAb/L98R structure in the resting state. DMPC lipid molecules are shown as yellow sticks to indicate the membrane bilayer.

Structure of Na V Ab/L98R. (A) Crystal structure of NaVAb/L98R with the mutation shown in red. (B) Close-up view of NaVAb/L98R structure in the activated state (teal). Side chains of residues L98R (red), Glu32, 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). The S3–S4 loop and the side chain of L98R are disordered. (C) Comparison of NaVAb/L98R structure (teal) with the structure of NaVAb WT (light orange). A hypothetical model for the L98R side chain (red) is illustrated to indicate a favorable rotamer that does not clash with the S3–S4 loop. NaVAb/I217C (PDB accession no. 3RVY) was used for the comparison as WT because the S3–S4 loop was not modeled in NaVAbΔ28 (PDB accession no. 6MWA). (D) Homology model of NaVAb/L98R structure in the resting state. DMPC lipid molecules are shown as yellow sticks to indicate the membrane bilayer.

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