Trypsin-like Serine Protease (Ser190 site)

Trypsin-like serine proteases are a family of enzymes that cleave peptide bonds after lysine or arginine residues. The Ser190 site refers to proteases within this family that have a serine residue at position 190 in their S1 binding pocket. This structural difference allows for the design of selective inhibitors, particularly halo-substituted amidines which show up to 220-fold selectivity for Ser190 over Ala190 enzymes. These proteases are involved in diverse biological processes including digestion, blood coagulation, immune responses, and are implicated in diseases such as thrombosis and cancer, making them important drug targets.

Inhibition of serine protease activity