Article
Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR1 or protein C.
Annals of the New York Academy of Sciences - 1 Jan 2001
Ayala Y M, Arosio D, Di Cera E
Abstract excerpt
W215 is a highly conserved residue that shapes the S3 and S4 specificity sites of thrombin. Replacement of W215 with Phe produces modest effects on thrombin function, whereas the W215Y replacement significantly compromises the amidolytic activity toward synthetic and natural substrates. Replacement of W215 with Ala reduces fibrinogen and PAR4 cleavage 500-fold and 280-fold, respectively. On the other hand, the...
Topics
- Fibrinogen
- Hydrolysis
- Mutation
- Protein C
- Receptors, Cell Surface
- Thrombin