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Atypical Muscarinic Allosteric Modulation: Cooperativity between Modulators and Their Atypical Binding Topology in Muscarinic M2 and M2/M5 Chimeric Receptors
The atypical actions of tacrine and Duo3 involve different modes of receptor interaction, but their sites of attachment seem to be the “common” allosteric binding domain at the entrance to the orthosteric ligand binding pocket of the M2-receptor. Expand
Allosteric site on muscarinic acetylcholine receptors: identification of two amino acids in the muscarinic M2 receptor that account entirely for the M2/M5 subtype selectivities of some structurally
Two amino acids account entirely for the (approximately 100-fold) M2/M5 selectivity of the alkane-bisammonium and the caracurine V type allosteric ligands at NMS-free M2 receptors. Expand
A model of the human M2 muscarinic acetylcholine receptor
The M2 muscarinic acetylcholine receptor belongs to the family of rhodopsin like G-Protein Coupled Receptors and bears an orthosteric binding site that is mediated by structurally different ligands such as gallamine, caracurine V salts or W84 (a hexamethonium-derivative). Expand
Different Environments for a Realistic Simulation of GPCRs‐Application to the M2 Muscarinic Receptor
A model of the human M2 muscarinic receptor was taken as an example for a class A G‐protein coupled receptor to explore the influence of different environments in a molecular dynamics simulationExpand