[HTML][HTML] Agonist recognition by proteinase-activated receptor 2 and thrombin receptor: importance of extracellular loop interactions for receptor function
DJ Lerner, M Chen, T Tram, SR Coughlin - Journal of Biological Chemistry, 1996 - ASBMB
Thrombin receptor and proteinase-activated receptor 2 (PAR2) define a family of G protein-
coupled receptors that are activated by a novel proteolytic mechanism. Specific cleavage of
their amino-terminal exodomains unmasks a new amino terminus which then serves as a
tethered ligand, docking intramolecularly to the body of the receptor to effect signaling.
Identification of the docking interactions between tethered ligand domain and receptor is
critical for understanding transmembrane signaling by these receptors. Synthetic" agonist …
coupled receptors that are activated by a novel proteolytic mechanism. Specific cleavage of
their amino-terminal exodomains unmasks a new amino terminus which then serves as a
tethered ligand, docking intramolecularly to the body of the receptor to effect signaling.
Identification of the docking interactions between tethered ligand domain and receptor is
critical for understanding transmembrane signaling by these receptors. Synthetic" agonist …