Type: | Domain | Name: | Antistasin-like domain |
Description: | Antistatin is a small, disulphide cross-linked serine protease inhibitor isolated from the salivary glands of the Mexican leech. It is a potentanticoagulant by virtue of its ability to inhibit factor Xa in the coagulation cascade. Antistatin also exhibits a strong antimetastatic activity. Itcontains internal repeats of a 25-26 amino acid sequence with a highly conserved pattern of 6 cysteine (Cys) and 2 glycine residues []. Manymetazoan proteins share sequence homology with this antistasin-like domain. The unique physical properties of these related Cys-rich proteins (proteaseresistance; 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 beta-sheets and interacts with proteinases []. | Short Name: | Antistasin-like |