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Article

How a Fragment Draws Attention to Selectivity Discriminating Features between the Related Proteases Trypsin and Thrombin.

Journal of medicinal chemistry - 11 Feb 2021

Sandner Anna, Ngo Khang, Schiebel Johannes, Pizarroso Angela Ilse Marca, Schmidt Linda, Wenzel Benjamin, Steinmetzer Torsten, Ostermann Andreas, Heine Andreas, Klebe Gerhard

Abstract excerpt

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...

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Identifiers

PMID: 33471524
DOI: 10.1021/acs.jmedchem.0c01809

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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