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• W2081996507 abstract "Agonists, including the neurotransmitter acetylcholine (ACh), bind at two sites in the neuromuscular ACh receptor channel (AChR) to promote a reversible, global change in protein conformation that regulates the flow of ions across the muscle cell membrane. In the synaptic cleft, ACh is hydrolyzed to acetate and choline. Replacement of the transmitter's ester acetyl group with a hydroxyl (ACh→choline) results in a + 1.8 kcal/mol reduction in the energy for gating generated by each agonist molecule from a low- to high-affinity change of the transmitter binding site (ΔG(B)). To understand the distinct actions of structurally related agonist molecules, we measured ΔG(B) for 10 related choline derivatives. Replacing the hydroxyl group of choline with different substituents, such as hydrogen, chloride, methyl, or amine, increased the energy for gating (i.e., it made ΔG(B) more negative relative to choline). Extending the ethyl hydroxide tail of choline to propyl and butyl hydroxide also increased this energy. Our findings reveal the amount of energy that is available for the AChR conformational change provided by different, structurally related agonists. We speculate that a hydrogen bond between the choline hydroxyl and the backbone carbonyl of αW149 positions this agonist's quaternary ammonium group so as to reduce the cation-π interaction between this moiety and the aromatic groups at the binding site." @default.
• W2081996507 created "2016-06-24" @default.
• W2081996507 creator A5045534329 @default.
• W2081996507 creator A5050511467 @default.
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• W2081996507 date "2013-02-01" @default.
• W2081996507 modified "2023-09-30" @default.
• W2081996507 title "Energy for Wild-Type Acetylcholine Receptor Channel Gating from Different Choline Derivatives" @default.
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• W2081996507 doi "https://doi.org/10.1016/j.bpj.2012.11.3833" @default.
• W2081996507 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3566445" @default.
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