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- W1999182346 abstract "Activation of voltage-gated sodium (Nav) channels initiates and propagates action potentials in electrically excitable cells. The -scorpion toxin CssIV traps a voltage-sensor of Nav channels in its activated state via a voltage-sensor trapping mechanism and thus shifts their voltage dependence of activation to more negative membrane potentials. The SS2-S6 linker of the pore domain in domain III (IIISS2-S6) is crucial in determining the action of CssIV upon Nav channels. We found that five substitutions at four amino acid residues in IIISS2-S6 markedly alter voltage-sensor trapping current (IVST) by a recombinant toxin derivative, CssIVE15A. These residues are concentrated in the region between N1436 and D1445 and form a discontinuous interaction site. Three of them (E1438A, D1445A and D1445Y) markedly decrease IVST, whereas the other two (N1436G and L1439A) markedly increase IVST. N1436G increases binding affinity of CssIVE15A to Nav channels in the resting state, whereas L1439A increases the efficacy of trapping the activated voltage-sensor by the prebound toxin. Time courses of voltage sensor trapping for the WT and mutant channels fit an allosteric kinetic model that includes a lower affinity resting state and a higher affinity activated/trapped state. Structural modeling suggests that the IIISS2-S6 is in close proximity to the IIS1-S2 and IIS3-S4 linkers in 3D space and that the bound toxin sits in a cleft formed by these three extracellular loops. Our results define the molecular map of a third interacting component of the -scorpion toxin receptor site of mammalian Nav channels and provide new molecular details of the voltage-sensor trapping mechanism of toxin action." @default.
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- W1999182346 date "2012-01-01" @default.
- W1999182346 modified "2023-09-27" @default.
- W1999182346 title "Mapping the Receptor Sites for a β-Scorpion Toxin on the Pore Module in Domain III of Voltage-Gated Sodium Channels" @default.
- W1999182346 doi "https://doi.org/10.1016/j.bpj.2011.11.1782" @default.
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