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. Author manuscript; available in PMC: 2013 Jun 20.
Published in final edited form as: Nature. 2012 Dec 9;492(7429):387–392. doi: 10.1038/nature11701

Figure 1. PAR1 activation and overall structure of human PAR1 complex with antagonist vorapaxar.

Figure 1

a, Thrombin cleaves PAR1 N-terminus and exposes a new N-terminal peptide SFLLRN, which can bind to and activate the transmembrane core of PAR1. PAR1 can activate several G proteins including Gi, G12/13 and Gq. b, Overall view of the human PAR1 structure and the extracellular surface. The receptor is shown in blue ribbon and vorapaxar is shown as green spheres. Monoolein is shown in orange, water in red. The disulfide bond is shown as a yellow stick. c, Surface view of the ligand-binding pocket viewed from two different perspectives. The vorapaxar binding pocket is close to the extracellular surface but not well exposed to the extracellular solvent.