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 language | English |
|---|---|
| Pages (from-to) | 385-392 |
| Number of pages | 8 |
| Journal | Biochemistry International |
| Volume | 28 |
| Issue number | 3 |
| Publication status | Published - 1992 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Serine proteinase inhibition by the cyclic thiolic compound YS3025 : A crystallographic study. / Rizzi, M.; Casale, E.; Coda, A.; La Rosa, C.; Ascenzi, P.; Luisetti, M.; Bolognesi, M.
In: Biochemistry International, Vol. 28, No. 3, 1992, p. 385-392.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Serine proteinase inhibition by the cyclic thiolic compound YS3025
T2 - A crystallographic study
AU - Rizzi, M.
AU - Casale, E.
AU - Coda, A.
AU - La Rosa, C.
AU - Ascenzi, P.
AU - Luisetti, M.
AU - Bolognesi, M.
PY - 1992
Y1 - 1992
N2 - 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).
AB - 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).
UR - http://www.scopus.com/inward/record.url?scp=0026462207&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026462207&partnerID=8YFLogxK
M3 - Article
C2 - 1482382
AN - SCOPUS:0026462207
VL - 28
SP - 385
EP - 392
JO - Biochemistry and Molecular Biology International
JF - Biochemistry and Molecular Biology International
SN - 1039-9712
IS - 3
ER -