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• W2158150436 abstract "We measured the influence of gallamine on the functional responses and binding properties of selected agonists at the M₂ muscarinic receptor and analyzed the data within the context of the allosteric ternary complex model. Our analysis showed that gallamine modified agonist affinity without influencing efficacy. To explain this behavior, we investigated the allosteric ternary complex model at a deeper level of analysis to assess allosterism in terms of the differential affinity of gallamine for ground and active states of the receptor. Our simulations showed that two-state models based on a single orthosteric site for the agonist linked to an allosteric site for gallamine could not account for affinity-only modulation, even if multiple conformations of ground and active states were considered. We also expanded the tandem two-site model (<i>J Biol Chem</i> 275:18836–18844, 2000) within the context of the allosteric ternary complex model and analyzed the resulting hybrid model at the level of receptor states. This model posits that the agonist first binds to a relay site and then shuttles to the activation site to turn on the receptor. If it is assumed that allosterism occurs at the relay site and not the activation site, then this model can account for affinity-only modulation in a manner consistent with the allosteric ternary complex model." @default.
• W2158150436 created "2016-06-24" @default.
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• W2158150436 date "2008-02-27" @default.
• W2158150436 modified "2023-09-25" @default.
• W2158150436 title "Two-State Models and the Analysis of the Allosteric Effect of Gallamine at the M₂Muscarinic Receptor" @default.
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• W2158150436 doi "https://doi.org/10.1124/jpet.108.136960" @default.
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