Thrombin reveals new faces with a tiny trick

The study by Dei Rossi et al. [10] demonstrates that thrombin’s interaction specificity with substrates and inhibitors is predominantly dictated by the amino acid at the P1 position. The S1 pocket’s structural flexibility and size allow for a “chymotrypsin-like” specificity, even accommodating aromatic residues. These findings provide critical insights into understanding thrombin function and its potential for therapeutic targeting.