Guy H R
Cell Mol Neurobiol. 1981 Sep;1(3):231-58. doi: 10.1007/BF00710680.
Models of the protein structure of agonist-, competitive antagonist-, and snake neurotoxin-binding sites were designed using the sequence of the first 54 residues of the acetylcholine receptor (AChR) alpha subunit from Torpedo californica. These models are based on the premise that the N-terminal portions of the subunits form the outermost extracellular surface of the AChR and that agonists bind to this portion. The models were developed by predicting the secondary structure of the alpha-subunit N-terminal segment from its sequence, then using these predictions to fold the segment into tertiary structures that should bind snake neurotoxins, agonists, and antagonists. Possible gating mechanisms and quaternary structures are suggested by the proposed tertiary structures of the subunits. Experiments are suggested to test aspects of the models.
利用加州电鳐乙酰胆碱受体（AChR）α亚基前54个残基的序列，设计了激动剂、竞争性拮抗剂和蛇神经毒素结合位点的蛋白质结构模型。这些模型基于这样的前提：亚基的N端部分形成AChR最外层的细胞外表面，且激动剂与该部分结合。通过从α亚基N端片段的序列预测其二级结构，然后利用这些预测将该片段折叠成应能结合蛇神经毒素、激动剂和拮抗剂的三级结构，从而构建了这些模型。亚基的三级结构模型提示了可能的门控机制和四级结构。文中还建议进行实验以测试模型的各个方面。
