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. 2018 Sep 6;150(10):1360–1372. doi: 10.1085/jgp.201711979

Figure 7.

Figure 7. An allosteric network at the M4 mAChR. (A) Previous studies on the M4 mAChR have identified residues that either disrupt the binding of LY2033298 or alter the cooperativity between the allosteric and orthosteric site. These residues are shown in pink, modeled on to an active-state M4 mAChR homology model (white) based on the M2•iperoxo•LY2119620 crystal structure (Protein Data Bank accession no. 4MQT; Nawaratne et al., 2010; Leach et al., 2011; Thal et al., 2016). Views from the side (A) and extracellular surface (B) are shown.

An allosteric network at the M4 mAChR. (A) Previous studies on the M4 mAChR have identified residues that either disrupt the binding of LY2033298 or alter the cooperativity between the allosteric and orthosteric site. These residues are shown in pink, modeled on to an active-state M4 mAChR homology model (white) based on the M2•iperoxo•LY2119620 crystal structure (Protein Data Bank accession no. 4MQT; Nawaratne et al., 2010; Leach et al., 2011; Thal et al., 2016). Views from the side (A) and extracellular surface (B) are shown.