Serine proteinase inhibition by the cyclic thiolic compound YS3025: A crystallographic study

M. Rizzi, E. Casale, A. Coda, C. La Rosa, P. Ascenzi, M. Luisetti, M. Bolognesi

Research output: Contribution to journalArticlepeer-review

Abstract

In order to unravel the serine proteinase inhibition mechanism by cyclic thiolic compounds, the X-ray crystal structure of bovine α-chymotrypsin inhibited by 3-[2-(2-thiophencarboxythio)]propanoyl-4-thioazolidin carboxylic acid (YS3025) has been studied by means of difference Fourier techniques and refined at 2.8Å resolution (R-factor = 0.174). The thiophencarbonyl moiety of YS3025 is covalently linked, in the acyl-enzyme complex, to Ser195 OG atom of bovine α-chymotrypsin, and located at the entrance of the proteinase primary specificity subsite (S1). The present data confirm previous hypotheses raised on the inhibition mechanism of serine proteinases, based on solution studies of human leukocyte elastase in the presence of the YS3025 parent compound 2-[3-thiophencarboxythio]-N-[dihydro-2(3H)thiophenone-3-il]-propionamide (MR889).

Original languageEnglish
Pages (from-to)385-392
Number of pages8
JournalBiochemistry International
Volume28
Issue number3
Publication statusPublished - 1992

ASJC Scopus subject areas

  • Biochemistry

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