Article
Allosteric modulation of the activity of thrombin.
The Biochemical journal - 15 Jan 1997
Duffy E J, Angliker H, Le Bonniec B F, Stone S R
Abstract excerpt
Substrates containing a P3 aspartic residue are in general cleaved poorly by thrombin. This may be partly due to an unfavourable interaction between the P3 aspartate and Glu192 in the active site of thrombin. In Protein C activation and perhaps also thrombin receptor cleavage, binding of ligands at the anion-binding exosite of thrombin seems to improve the activity of thrombin with substrates containing a P3...
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