Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy

FEBS Lett. 2003 Nov 27;555(1):91-5. doi: 10.1016/s0014-5793(03)01084-6.

Abstract

The nicotinic acetylcholine (ACh) receptor is the transmitter-gated ion channel at the nerve/muscle synapse. Electron microscopical experiments on isolated postsynaptic membranes have determined the structure of this channel and how the structure changes upon activation. When ACh enters the ligand-binding domain it initiates rotations of the protein chains on opposite sides of the entrance to the membrane-spanning pore. These rotations are communicated to the pore-lining alpha-helices and open the gate--a constricting hydrophobic girdle at the middle of the membrane--by breaking it apart. The movements are small and involve energetically favourable displacements parallel to the membrane plane.

Publication types

  • Review

MeSH terms

  • Animals
  • Electric Organ / metabolism
  • In Vitro Techniques
  • Ion Channel Gating
  • Microscopy, Electron
  • Models, Molecular
  • Protein Conformation
  • Protein Subunits
  • Receptors, Nicotinic / chemistry*
  • Receptors, Nicotinic / metabolism
  • Receptors, Nicotinic / ultrastructure*
  • Rotation
  • Torpedo

Substances

  • Protein Subunits
  • Receptors, Nicotinic