4hg9

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Template:STRUCTURE 4hg9

Contents 1 Crystal structure of AhV_bPA, a basic PLA2 from Agkistrodon halys pallas venom 2 Function 3 About this Structure 4 See Also 5 Reference

Crystal structure of AhV_bPA, a basic PLA2 from Agkistrodon halys pallas venom

Function

[PA2BB_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]}

About this Structure

4hg9 is a 4 chain structure with sequence from Gloydius halys. Full crystallographic information is available from OCA.

See Also

• Phospholipase A2

Reference

1. ↑ Faure G, Gowda VT, Maroun RC. Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics. BMC Struct Biol. 2007 Dec 6;7:82. PMID:18062812 doi:http://dx.doi.org/10.1186/1472-6807-7-82
2. ↑ Zhao K, Zhou Y, Lin Z. Structure of basic phospholipase A2 from Agkistrodon halys Pallas: implications for its association, hemolytic and anticoagulant activities. Toxicon. 2000 Jul;38(7):901-16. PMID:10728829