Residues Responsible for the Selectivity of α-Conotoxins for Ac-AChBP or nAChRs
AbstractNicotinic acetylcholine receptors (nAChRs) are targets for developing new drugs to treat severe pain, nicotine addiction, Alzheimer disease, epilepsy, etc. α-Conotoxins are biologically and chemically diverse. With 12–19 residues and two disulfides, they can be specifically selected for different nAChRs. Acetylcholine-binding proteins from Aplysia californica (Ac-AChBP) are homologous to the ligand-binding domains of nAChRs and pharmacologically similar. X-ray structures of the α-conotoxin in complex with Ac-AChBP in addition to computer modeling have helped to determine the binding site of the important residues of α-conotoxin and its affinity for nAChR subtypes. Here, we present the various α-conotoxin residues that are selective for Ac-AChBP or nAChRs by comparing the structures of α-conotoxins in complex with Ac-AChBP and by modeling α-conotoxins in complex with nAChRs. The knowledge of these binding sites will assist in the discovery and design of more potent and selective α-conotoxins as drug leads. View Full-Text
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Lin, B.; Xiang, S.; Li, M. Residues Responsible for the Selectivity of α-Conotoxins for Ac-AChBP or nAChRs. Mar. Drugs 2016, 14, 173.
Lin B, Xiang S, Li M. Residues Responsible for the Selectivity of α-Conotoxins for Ac-AChBP or nAChRs. Marine Drugs. 2016; 14(10):173.Chicago/Turabian Style
Lin, Bo; Xiang, Shihua; Li, Mengsen. 2016. "Residues Responsible for the Selectivity of α-Conotoxins for Ac-AChBP or nAChRs." Mar. Drugs 14, no. 10: 173.
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