| Title : Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy - Unwin_2003_FEBS.Lett_555_91 |
| Author(s) : Unwin N |
| Ref : FEBS Letters , 555 :91 , 2003 |
|
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. |
| PubMedSearch : Unwin_2003_FEBS.Lett_555_91 |
| PubMedID: 14630325 |
Unwin N (2003)
Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy
FEBS Letters
555 :91
Unwin N (2003)
FEBS Letters
555 :91