Fig. 7: Cryo-EM structure of the GB88:PAR2-Gαq-scFv16 complex.
From: Structural basis for the activation of proteinase-activated receptors PAR1 and PAR2
A Cryo-EM density map of the GB88:PAR2-Gαq-scFv16 complex perpendicular to the membrane (B). Model of GB88:PAR2-Gαq-scFv16 complex shown in cartoon representation. C Cartoon representation of PAR2 (green) with GB88 bound (cyan sticks) viewing from the extracellular side of the membrane with TMs and ECLs labeled. D GB88 (cyan sticks) is shown within the orthosteric pocket of PAR2 (slabbed surface). The GB88 cryo-EM map is shown as blue mesh at 5.0 sigma (E). GB88 (cyan) bound to the orthosteric pocket of PAR2 highlighting key residues (yellow) and H-bonds formed between the ligand and receptor. F Structural overlay (receptor not shown) of the GB88 and the tethered agonist structures to demonstrate GB88’s mimicry of the tethered ligand within the orthosteric site. GB88 is shown in cyan with chemical substituents labeled also in cyan. The tethered ligand is shown in green with residues labeled also in green.
