Viperin |
VIPFVASVAAEMQHVYCAASRKC |
natural killer cell lectin-like receptor 2A |
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Viperistatin isolated from the venom Vipera palaestinae (Palestine viper) (Pseudocerastes palaestinae) represents one of the shortest known snake venom monomeric disintegrins. Its amino acid sequence (CTTGPCCRQCKLKPAGTTCWKTSRTSHYCTGKSCDCPVYQG) differs from Obtustatin in three residues at position 24 (within the integrin binding loop), 38 (hydrophobic core) and 40 (C-terminal region). As a selective inhibitor of integrin-alpha-1 / integrin-beta-1 viperistatin is about 25-fold more potent than Obtustatin in inhibiting the binding of this integrin to collagen type-4. (Kisiel et al, 2004).
Socha et al (2006) have reported that the adhesive function of eosinophils to collagen type-4 is inhibited by viperistatin. The protein is more potent than Obtustatin
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