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. Author manuscript; available in PMC: 2016 Sep 15.
Published in final edited form as: Eur J Pharmacol. 2015 May 14;763(0 0):196–205. doi: 10.1016/j.ejphar.2015.05.013

Fig. 5.

Fig. 5

Class C GPCR structure, ligand binding sites and ligand selectivity. (A) Structure of the homodimeric extracellular venus flytrap domain of mGlu1 with a bound agonist glutamate shown in stick and space-filling representation in the orthosteric binding site (PDB: 1EWK). Glycans and disulfide bonds are shown in stick representation. (B) Structure of the mGlu1 7TM domain with a bound negative allosteric modulator FITM shown in stick and space-filling representation (PDB: 4OR2). Cholesterol molecules at the interface of the 7TM “homodimer” and disulfide bonds are shown in stick representation. (C) Superposition of the class C mGlu1 7TM domain and the class A dopamine D3 receptor with a bound antagonist eticlopride (PDB: 3PBL) viewed from the extracellular side. FITM is colored yellow and eticlopride magenta. FITM, eticlopride, and disulfide bonds are shown in stick representation. (D) Superposition of the mGlu1 and mGlu5 (PDB: 4OO9) 7TM structures highlighting a subtype selectivity determinant for negative allosteric modulator binding. FITM is colored green and mavoglurant is slate blue.