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- W289388518 abstract "The cys-loop family of ligand-gated ion channels plays an important role in the chemical-to-electrical transduction of neuronal signaling. The well-studied α7-nAChR may be linked to nicotine addiction, and shows possible genetic linkages to such diseases as Alzheimer's and schizophrenia. The discovery of a homologous soluble snail acetylcholine binding protein (AChBP) provided a structural surrogate of the extracellular ligand-binding domain; however, the binding protein, despite the requisite ligand properties, shows only 30% residue identity with the nicotinic receptor family. Here we show systematic mutations of the soluble Aplysia californica towards the α7-nAChR with simultaneous analysis of binding affinities. Key constructs were subsequently characterized using classical α7-nAChR selective ligands such as α-bungarotoxin, (+)-epibatidine, and methyllycaconitine, as well as crystal structures have been obtained for some of the intermediate constructs. (Support: U01-NS 05846, GM07752-29)" @default.
- W289388518 created "2016-06-24" @default.
- W289388518 creator A5004460355 @default.
- W289388518 creator A5013129078 @default.
- W289388518 date "2009-04-01" @default.
- W289388518 modified "2023-10-05" @default.
- W289388518 title "Alpha‐7 Nicotinic Acetylcholine Receptor (nAChR) Characteristics on the Acetylcholine Binding Protein" @default.
- W289388518 doi "https://doi.org/10.1096/fasebj.23.1_supplement.942.4" @default.
- W289388518 hasPublicationYear "2009" @default.
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