Thrombin receptor
There are three known thrombin receptors termed PAR1, PAR3 and PAR4 (PAR for protease-activated receptor). [1]
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
- ^ "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.
.svg){kind=small} | This biochemistry article is a stub. You can help Wikipedia by expanding it. |