Probing the structure of the uncoupled nicotinic acetylcholine receptor

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• 作者：Jiayin Sun ; J. Frederique Comeau ; John E. Baenziger ; ^{John.Baenziger@uottawa.ca}
• 关键词：ACh ; acetylcholine ; α-BTX ; α-bungarotoxin ; Carb ; carbamylcholine ; Chol ; cholesterol ; ECD ; extracellular domain ; ELIC ; Erwinia ligand-gated ion channel ; GLIC ; Gloebacter ligand-gated ion channel ; nAChR ; nicotinic acetylcholine receptor ; PA ; 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidic acid ; PC ; 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine ; pLGIC ; pentameric ligand-gated ion channel ; TID ; 3-trifluoromethyl-3-(m-[125I]iodophenyl) diazirine ; TMD ; transmembrane domain
• 刊名：Biochimica et Biophysica Acta (BBA) - Biomembranes
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1859
• 期：2
• 页码：146-154
• 全文大小：789 K
• 卷排序：1859

文摘

The uncoupled nAChR does not undergo agonist-induced conformational transitions. The agonist site exhibits resting state-like agonist binding affinity. The transmembrane pore does not bind typical fluorescent channel blockers. A distinct conformation of the uncoupled pore may be similar to that of ELIC.