Thrombin receptor

There are three known thrombin receptors (ThrR[1]), termed PAR1, PAR3 and PAR4 (PAR for protease-activated receptor). [2]

"ThrR" redirects here. For other uses, see THRR (disambiguation).

These receptors are members of the 7-transmembrane g protein-coupled family of receptors, however, their method of activation is unique. Thrombin, a serine protease, binds to and cleaves the extracellular N-terminal domain of the receptor. A tethered ligand corresponding to the new N-terminus, SFLLRN, is then unmasked, binding to the second extracellular loop of the receptor and activating it.

References
  1. A L Darrow, W P Fung-Leung, R D Ye, R J Santulli, W M Cheung, C K Derian, C L Burns, B P Damiano, L Zhou, C M Keenan, P A Peterson, P Andrade-Gordon (December 1996). "Biological consequences of thrombin receptor deficiency in mice". Thrombosis and Haemostasis. 76 (6): 860–6. PMID 8972001.CS1 maint: uses authors parameter (link)
  2. "Thrombin receptors and their antagonists: an update on the patent literature". Expert Opin Ther Pat. 20 (7): 875–84. Jul 2010. doi:10.1517/13543776.2010.487864. PMID 20450349. Retrieved 8 April 2013.
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