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The cystatins: Protein inhibitors of cysteine proteinases
Author(s) -
Turk Vito,
Bode Wolfram
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80804-c
Subject(s) - cystatin , cysteine , biochemistry , cysteine proteinase inhibitors , serine proteinase inhibitors , chemistry , serine , superfamily , mechanism (biology) , biology , cystatin c , enzyme , gene , serine protease , apoptosis , programmed cell death , renal function , caspase , protease , philosophy , epistemology
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.