Fig. 5: Mapping of mutagenesis studies for BTX-B on the structure of rNaV1.5c. | Nature Communications

Fig. 5: Mapping of mutagenesis studies for BTX-B on the structure of rNaV1.5c.

From: Dual receptor-sites reveal the structural basis for hyperactivation of sodium channels by poison-dart toxin batrachotoxin

Fig. 5

a Residues near Site IIB2 (cyan sticks) from DIII (yellow) and DIV (red) that have been identified for BTX binding from mutagenesis studies27,36,49. The side chains are shown as sticks overlaid with transparent van der Waals spheres. b Location of residues N377 to E418 (teal) that includes DI-S6 of rNaV1.5c near Site IIB1 (bright green stick). This fragment is equivalent to residues N388 to E429 in rNaV1.2 that has been shown to interact with azido BTX-B derivative by photoaffinity labeling23. c Residues near Site IIB1 (bright green stick) from DI (blue) and DIV (red) that have been identified for BTX binding from mutagenesis studies25,36,50 The side chains are shown as sticks overlaid with transparent van der Waals spheres. Y1769 is within 5 Å from the BTX-B but is not significantly involved in the binding based on mutagenesis studies.

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