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Interactions of orthosteric and allosteric ligands with [3H]dimethyl-W84 at the common allosteric site of muscarinic M2 receptors.
It is suggested that these atypical ligands either bind to the two known spatially separated allosteric sites on muscarinic receptors with positive cooperativity or their binding to the common allosterics site modulates receptor-receptor interactions such that homotropic positive cooperateativity within a dimer or higher oligomer is generated. 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
[Muscarinic acetylcholine receptors as target structures for drugs. Old and new mechanisms].