Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures.

By P. Celie, Sarah E. van Rossum-Fikkert, W. V. van Dijk, K. Brejc, A. Smit, T. Sixma. Neuron, 2004

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Refined structure of the nicotinic acetylcholine receptor at 4A resolution. (2005, background): “Clearly, the earlier identification was mistaken, and the actual binding sites are closer to the g and d-subunit interfaces in locations equivalent to those in AChBP.”
Single-Channel Behavior of Heteromeric α1β Glycine Receptors: An Attempt to Detect a Conformational Change before the Channel Opens (2004, background): “Changes at the binding site precede channel opening, and the two may be linked by a wave of conformational changes in which successive discrete subdomains between the binding site and the pore move in a sequence of rigid body movements (Chakrapani et al., 2004).”
Mammalian Nicotinic Acetylcholine Receptors: From Structure to Function (2009, background): “In addition to the Cys-Cys pair, other residues required for ligand binding are predominantly hydrophobic aromatic amino acids, including aTyr 93, αTrp 149, αTyr 190, and αTyr 198 (80,229,431).”
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations (2005, background): “They are a7 and a3b2 nAChR selective, with lower affinity for ImII (Ellison et al, 2004).”