Fig. 1: Cryo-EM structure of the PAR1-Gαq-scFv16 tethered peptide agonist complex. | Nature Communications

Fig. 1: Cryo-EM structure of the PAR1-Gαq-scFv16 tethered peptide agonist complex.

From: Structural basis for the activation of proteinase-activated receptors PAR1 and PAR2

Fig. 1

A Cryo-EM density map of PAR1-Gαq-scFv16 with tethered ligand. (PAR1, blue; Gαq, teal; Gβ, yellow; Gγ, purple; scFv16, gray). B Cartoon representation of PAR1-Gαq-scFv16 with tethered ligand bound. Inset: tethered ligand (yellow sticks) is shown within the orthosteric pocket of PAR1 (slabbed surface). The tethered ligand cryo-EM map is shown as blue mesh at 5.0 sigma. C Cartoon representation of PAR1 (blue) with the tethered ligand bound (yellow sticks) viewing from the extracellular side of the membrane with TMs and ECLs labeled. D H-bond interactions between the tethered ligand (yellow sticks) and PAR1 orthosteric residues (orange sticks).

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