Emerging structure of the nicotinic acetylcholine receptors.
The conversion of acetylcholine binding into ion conduction across the membrane is becoming more clearly understood in terms of the structure of the receptor and its transitions. A high-resolution structure of a protein that is homologous to the extracellular domain of the receptor has revealed the binding sites and subunit interfaces in great detail. Although the structures of the membrane and cytoplasmic domains are less well determined, the channel lining and the determinants of selectivity have been mapped. The location and structure of the gates, and the coupling between binding sites and gates, remain to be established.
Karlin
Arthur
A
Center for Molecular Recognition, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA. ak12@columbia.edu
D000109:Acetylcholine / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites / Q000502:physiology; D002352:Carrier Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D007473:Ion Channels / Q000378:metabolism*; D008024:Ligands; D017434:Protein Structure, Tertiary / Q000502:physiology; D011978:Receptors, Nicotinic / Q000378:metabolism*; D009435:Synaptic Transmission / Q000502:physiology*
C428944:AChBP protein, Lymnaea; D002352:Carrier Proteins; D007473:Ion Channels; D008024:Ligands; D011978:Receptors, Nicotinic; D000109:Acetylcholine