The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of an alpha helix lying on top of an anti-parallel beta sheet. The family is subdivided as described below.
Cystatins show similarity to fetuins, kininogens, histidine-rich glycoproteins and cystatin-related proteins.[2][3][4]
Cystatins mainly inhibit peptidase enzymes (another term for proteases) belonging to peptidase families C1 (papain family) and C13 (legumain family). They are known to mis-fold to form amyloid deposits and are implicated in several diseases.[citation needed]
^Salát J, Paesen GC, Rezácová P, Kotsyfakis M, Kovárová Z, Sanda M, et al. (July 2010). "Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata". The Biochemical Journal. 429 (1): 103–112. doi:10.1042/BJ20100280. PMC 3523712. PMID 20545626.; rendered with PyMOL
^Rawlings ND, Barrett AJ (January 1990). "Evolution of proteins of the cystatin superfamily". Journal of Molecular Evolution. 30 (1): 60–71. Bibcode:1990JMolE..30...60R. doi:10.1007/BF02102453. PMID 2107324. S2CID 33504413.
^Abrahamson M, Alvarez-Fernandez M, Nathanson CM (2003). "Cystatins". Biochemical Society Symposium. 70 (70): 179–199. doi:10.1042/bss0700179. PMID 14587292.
^Turk V, Bode W (July 1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Letters. 285 (2): 213–219. Bibcode:1991FEBSL.285..213T. doi:10.1016/0014-5793(91)80804-C. PMID 1855589. S2CID 40444629.
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