Functional determinants by which snake and cone snail toxins block the alpha 7 neuronal nicotinic acetylcholine receptors

J Physiol Paris. 1998 Apr;92(2):107-11. doi: 10.1016/s0928-4257(98)80146-0.

Abstract

Snakes and cone snails produce toxins which block muscular and/or neuronal nicotinic acetylcholine receptors (AChRs). This paper mostly focuses on the determinants by which a snake long chain curaremimetic toxin and the cone snail toxin ImI bind specifically to the alpha 7 neuronal receptor. In both cases, the site involves a small turn-like structure constrained by two half-cystines.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Charybdotoxin / chemistry
  • Charybdotoxin / pharmacology
  • Conotoxins*
  • Curare / analogs & derivatives
  • Curare / chemistry
  • Curare / pharmacology
  • Erabutoxins / chemistry
  • Erabutoxins / pharmacology
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Mollusk Venoms / chemical synthesis
  • Mollusk Venoms / chemistry*
  • Mollusk Venoms / pharmacology
  • Mutagenesis, Site-Directed
  • Neurons / physiology*
  • Nicotinic Antagonists / chemical synthesis
  • Nicotinic Antagonists / chemistry*
  • Nicotinic Antagonists / pharmacology
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Oligopeptides / pharmacology
  • Receptors, Nicotinic / chemistry*
  • Receptors, Nicotinic / metabolism*
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Sequence Alignment
  • Snails
  • Snake Venoms / chemical synthesis
  • Snake Venoms / chemistry*
  • Snake Venoms / pharmacology
  • alpha7 Nicotinic Acetylcholine Receptor

Substances

  • Chrna7 protein, human
  • Conotoxins
  • Mollusk Venoms
  • Nicotinic Antagonists
  • Oligopeptides
  • Receptors, Nicotinic
  • Recombinant Fusion Proteins
  • Snake Venoms
  • alpha7 Nicotinic Acetylcholine Receptor
  • Charybdotoxin
  • alpha-conotoxin ImI
  • Erabutoxins
  • Curare