Abstract:In the S1 pocket, the serine proteases thrombin and
trypsin commonly feature Asp189 and a Ala190Ser and Glu192Gln exchange.
Nevertheless, thrombin cleaves peptide chains solely after Arg, and
trypsin after Lys and Arg. Thrombin exhibits a Na+-binding site next to Asp189, which
is missing in trypsin. The fragment benzylamine
shows direct H-bonding to Asp189 in trypsin, while in thrombin, it
forms an H-bond to Glu192. A series of fragments and expanded ligands
were studied against both enzymes and mutated varian… Show more
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