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Article

Understanding binding selectivity toward trypsin and factor Xa: the role of aromatic interactions.

ChemMedChem - 1 Mar 2007

Di Fenza Armida, Heine Andreas, Koert Ulrich, Klebe Gerhard

Abstract excerpt

A congeneric series of four bis-benzamidine inhibitors sharing a dianhydrosugar isosorbide scaffold in common has been studied by crystal structure analysis and enzyme kinetics with respect to their binding to trypsin and factor Xa. Within the series, aromatic interactions are an important determinant for selectivity discrimination among both serine proteases. To study the selectivity-determining features in...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17191291
DOI: 10.1002/cmdc.200600185

Provenance

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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