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The cystatins: Protein inhibitors of cysteine proteinases

FEBS Letters · 1991 · Vol. 285(2) · pp. 213–219
Vito TürkWolfram Bode

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.

Coagulation, Bradykinin, Polyphosphates, and AngioedemaLysosomal Storage Disorders ResearchCellular transport and secretionCystatinCysteineBiochemistryCysteine Proteinase InhibitorsSerine Proteinase InhibitorsChemistrySerineSUPERFAMILYMechanism (biology)Biology

MeSH terms

Amino Acid SequenceKininogensMolecular Sequence DataProtein ConformationCysteine Proteinase InhibitorsCystatinsMacromolecular SubstancesCystatin B
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References
Protein Inhibitors of Proteinases
Annual Review of Biochemistry · 1980 · 2,242 citations
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