Abstract
The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures, functions and evolutionary relationships. Although they differ in their molecular properties and biological distribution, they are structurally related proteins. All three inhibitory families, the stefins, the cystatins and the kininogens, are members of the same superfamily. Recently determined crystal structures of chicken cystatin and human stefin B established a new mechanism of interaction between cysteine proteinases and their inhibitors which is fundamentally different from the standard mechanism for serine proteinases and their inhibitors.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 3:43 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 15, 2023, 9:38 p.m.) |
Indexed | 2 days, 6 hours ago (Aug. 29, 2025, 5:43 a.m.) |
Issued | 34 years, 1 month ago (July 1, 1991) |
Published | 34 years, 1 month ago (July 1, 1991) |
Published Online | 23 years, 8 months ago (Dec. 17, 2001) |
Published Print | 34 years, 1 month ago (July 1, 1991) |
@article{Turk_1991, title={The cystatins: Protein inhibitors of cysteine proteinases}, volume={285}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(91)80804-c}, DOI={10.1016/0014-5793(91)80804-c}, number={2}, journal={FEBS Letters}, publisher={Wiley}, author={Turk, Vito and Bode, Wolfram}, year={1991}, month=jul, pages={213–219} }