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• W4281486568 abstract "Although the functional properties of ion channels are most accurately assessed using electrophysiological approaches, a number of experimental situations call for alternative methods. Here, working on members of the pentameric ligand-gated ion channel (pLGIC) superfamily, we focused on the practical implementation of, and the interpretation of results from, equilibrium-type ligand-binding assays. Ligand-binding studies of pLGICs are by no means new, but the lack of uniformity in published protocols, large disparities between the results obtained for a given parameter by different groups, and a general disregard for constraints placed on the experimental observations by simple theoretical considerations suggested that a thorough analysis of this classic technique was in order. To this end, we present a detailed practical and theoretical study of this type of assay using radiolabeled α-bungarotoxin, unlabeled small-molecule cholinergic ligands, the human homomeric α7-AChR, and extensive calculations in the framework of a realistic five-binding-site reaction scheme. Furthermore, we show examples of the practical application of this method to tackle two longstanding questions in the field: our results suggest that ligand-binding affinities are insensitive to binding-site occupancy and that mutations to amino-acid residues in the transmembrane domain are unlikely to affect the channel's affinities for ligands that bind to the extracellular domain." @default.
• W4281486568 created "2022-05-26" @default.
• W4281486568 creator A5004569758 @default.
• W4281486568 creator A5036527979 @default.
• W4281486568 date "2022-05-25" @default.
• W4281486568 modified "2023-10-18" @default.
• W4281486568 title "Probing function in ligand-gated ion channels without measuring ion transport" @default.
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• W4281486568 doi "https://doi.org/10.1085/jgp.202213082" @default.
• W4281486568 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35612603" @default.
• W4281486568 hasPublicationYear "2022" @default.
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