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.
De Cristofaro, R., Thrombin reveals new faces with a tiny trick, <<JOURNAL OF THROMBOSIS AND HAEMOSTASIS>>, 2025; 23 (4): 1203-1204. [doi:10.1016/j.jtha.2025.01.001] [https://hdl.handle.net/10807/311776]
Thrombin reveals new faces with a tiny trick
De Cristofaro, Raimondo
Conceptualization
2025
Abstract
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.
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