1u73

Structural highlights

Function

PA2A_BOTJR Snake venom phospholipase A2 (PLA2) that induces edema (activity that is inhibited by EDTA and dexamethasone), inhibits phospholipid-dependent collagen/ADP-induced platelet aggregation, possess hypotensive as well as anticoagulant activities. In addition, this enzyme shows bactericidal activity against E.coli and S.aureus. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.^{[1] [2]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Phospholipase A2 3D structures

References

1. ↑ Andriao-Escarso SH, Soares AM, Fontes MR, Fuly AL, Correa FM, Rosa JC, Greene LJ, Giglio JR. Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops jararacussu snake venom. Biochem Pharmacol. 2002 Aug 15;64(4):723-32. PMID:12167491
2. ↑ Roberto PG, Kashima S, Marcussi S, Pereira JO, Astolfi-Filho S, Nomizo A, Giglio JR, Fontes MR, Soares AM, Franca SC. Cloning and identification of a complete cDNA coding for a bactericidal and antitumoral acidic phospholipase A2 from Bothrops jararacussu venom. Protein J. 2004 May;23(4):273-85. PMID:15214498