Thrombin reveals new faces with a tiny trick

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