| Description | Antistatin is a small, disulphide cross-linked serine protease inhibitor isolated from the salivary glands of the Mexican leech. It is a potent anticoagulant by virtue of its ability to inhibit factor Xa in the coagulation cascade. Antistatin also exhibits a strong antimetastatic activity. It contains internal repeats of a 25-26 amino acid sequence with a highly conserved pattern of 6 cysteine (Cys) and 2 glycine residues [ ]. Many metazoan proteins share sequence homology with this antistasin-like domain. The unique physical properties of these related Cys-rich proteins (protease resistance; heat, chemical resilience) appear to stem from the common six Cys loop that is cross-linked by three disulfide bonds []. Disulfide linkages are between Cys1-Cys4, Cys2-Cys5, and Cys3-Cys6 [, ].The antistasin-like domain consists of very short antiparallel β-sheets and interacts with proteinases [ ]. | Name | Antistasin-like domain |
| Short Name | Antistasin-like | Type | Domain |
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