4hg9
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Crystal structure of AhV_bPA, a basic PLA2 from Agkistrodon halys pallas venom
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Structural highlights
FunctionPA2BB_GLOHA Snake venom phospholipase A2 (PLA2) that shows potent hemolytic activity, and exhibits medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 90 nM). It is one of the few phospholipases A2 capable of hydrolyzing the phospholipids of E.coli membranes in the presence of a bactericidal/permeability-increasing protein (BPI) of neutrophils. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[1] [2] See AlsoReferences
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This page was last modified 15:05, 20 September 2023.