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. 2017 Aug 20;42(3):67–83. doi: 10.1584/jpestics.D17-019

Fig. 3. The Nicotinic acetylcholine receptor. (A) The nAChR is an integral membrane protein embedded in the post synaptic membrane. (B) The α and β subunits are arranged in a homo or hetero-pentameric structure, with the ACh binding site lying at the interface between subunits, as denoted in red. (C) Each subunit has a large N-terminus, 4 transmembrane domains and a large intracellular loop. The ACh binding site is made up of 3 loops from the principal α-subunit and contact point from the β-subunit of the M1 domain. The position of the cysteine amino acids that form the critical disulphide loop are shown. (D) A functional nAChR contains five subunits with the second transmembrane domain lining the pore of the channel.

Fig. 3. The Nicotinic acetylcholine receptor. (A) The nAChR is an integral membrane protein embedded in the post synaptic membrane. (B) The α and β subunits are arranged in a homo or hetero-pentameric structure, with the ACh binding site lying at the interface between subunits, as denoted in red. (C) Each subunit has a large N-terminus, 4 transmembrane domains and a large intracellular loop. The ACh binding site is made up of 3 loops from the principal α-subunit and contact point from the β-subunit of the M1 domain. The position of the cysteine amino acids that form the critical disulphide loop are shown. (D) A functional nAChR contains five subunits with the second transmembrane domain lining the pore of the channel.