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

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.