Molecular mechanisms of neurotoxin action on voltage-gated sodium channels

Biochimie. Sep-Oct 2000;82(9-10):883-92. doi: 10.1016/s0300-9084(00)01174-3.

Abstract

Voltage-gated sodium channels are the molecular targets for a broad range of neurotoxins that act at six or more distinct receptor sites on the channel protein. These toxins fall into three groups. Both hydrophilic low molecular mass toxins and larger polypeptide toxins physically block the pore and prevent sodium conductance. Alkaloid toxins and related lipid-soluble toxins alter voltage-dependent gating of sodium channels via an allosteric mechanism through binding to intramembranous receptor sites. In contrast, polypeptide toxins alter channel gating by voltage sensor trapping through binding to extracellular receptor sites. The results of recent studies that define the receptor sites and mechanisms of action of these diverse toxins are reviewed here.

Publication types

  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Ion Channel Gating / drug effects*
  • Ion Channel Gating / physiology
  • Neurotoxins / pharmacology*
  • Protein Structure, Secondary
  • Sodium Channels / drug effects*
  • Sodium Channels / physiology

Substances

  • Neurotoxins
  • Sodium Channels