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• W2595542005 startingPage "1836" @default.
• W2595542005 abstract "Designing subtype-selective agonists for neuronal nicotinic acetylcholine receptors is a challenging and significant goal aided by intricate knowledge of each subtype’s binding patterns. We previously reported that in α6β2 receptors, acetylcholine makes a functional cation−π interaction with Trp149, but nicotine and TC299423 do not, suggesting a distinctive binding site. This work explores hydrogen binding at the backbone carbonyl associated with α6β2 Trp149. Substituting residue i + 1, Thr150, with its α-hydroxy analogue (Tah) attenuates the carbonyl’s hydrogen bond accepting ability. At α6(T150Tah)β2, nicotine shows a 24-fold loss of function, TC299423 shows a modest loss, and acetylcholine shows no effect. Nicotine was further analyzed via a double-mutant cycle analysis utilizing N′-methylnicotinium, which indicated a hydrogen bond in α6β2 with a ΔΔG of 2.6 kcal/mol. Thus, even though nicotine does not make the conserved cation−π interaction with Trp149, it still makes a functional hydrogen bond to its associated backbone carbonyl." @default.
• W2595542005 created "2017-03-23" @default.
• W2595542005 creator A5002660163 @default.
• W2595542005 creator A5024286952 @default.
• W2595542005 creator A5044058751 @default.
• W2595542005 date "2017-03-21" @default.
• W2595542005 modified "2023-10-17" @default.
• W2595542005 title "Probing for and Quantifying Agonist Hydrogen Bonds in α6β2 Nicotinic Acetylcholine Receptors" @default.
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• W2595542005 doi "https://doi.org/10.1021/acs.biochem.7b00213" @default.
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