The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits.
A binding site for the channel-blocking noncompetitive antagonist [3H]triphenylmethylphosphonium ([3H]TPMP+) was localized in the alpha-, beta- and delta-chains of the nicotinic acetylcholine receptor (AChR) from Torpedo marmorata electric tissue. The photolabel was found in homologous positions of the highly conserved sequence helix II, alpha 248, beta 254, and delta 262. The site of the photoreaction appears to not be affected by the functional state of the receptor. [3H]TPMP+ was found in position delta 262 independent of whether photolabeling was performed with the receptor in its resting, desensitized or antagonist state. A model of the AChR ion channel is proposed, according to which the channel is formed by the five helices II contributed by the five receptor subunits.
D000345:Affinity Labels; D000818:Animals; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D003488:Cyanogen Bromide; D004557:Electric Organ / Q000378:metabolism; D007473:Ion Channels / Q000032:analysis*; D008958:Models, Molecular; D009861:Onium Compounds; D010777:Photochemistry; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000302:isolation & purification*; D014101:Torpedo; D014320:Triphenylmethyl Compounds; D014357:Trypsin
D000345:Affinity Labels; D007473:Ion Channels; D009861:Onium Compounds; D011978:Receptors, Nicotinic; D014320:Triphenylmethyl Compounds; C011561:triphenylmethylphosphonium; D014357:Trypsin; D003488:Cyanogen Bromide