Phospholipase A2 homolog

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Function

Phospholipase A2 homolog or Basic phospholipase A2 homolog is a snake venom with phospholipase A2 (PLA2) sequence homology and structure homology which has almost no PLA2 activity, i.e., cleaving of fatty acids. The loss of PLA2 catalytic activity is due to the substitution of the conserved Asp49 in the active site by Lys49 in the homolog[1].

Disease

The venom causes severe muscle necrosis.

Structural highlights

The complex between PLA2 homolog and the inhibitor suramin shows the inhibitor interacting with both monomers. The water molecules are shown as red spheres. The location of PLA2 active site conserved Asp49 which is substituted by Lys in PLA2 homologs thus rendering PLA2[2].


Phospholipase A2 homolog dimer complex with inhibitor suramin, PEG400, pentaethylene glycol and sulfate (PDB code 4yv5)

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3D structures of phospholipase A2 homolog

Updated on 21-July-2024


References

  1. Lomonte B, Angulo Y, Sasa M, Gutierrez JM. The phospholipase A2 homologues of snake venoms: biological activities and their possible adaptive roles. Protein Pept Lett. 2009;16(8):860-76. doi: 10.2174/092986609788923356. PMID:19689412 doi:http://dx.doi.org/10.2174/092986609788923356
  2. Salvador GH, Dreyer TR, Cavalcante WL, Matioli FF, Dos Santos JI, Velazquez-Campoy A, Gallacci M, Fontes MR. Structural and functional evidence for membrane docking and disruption sites on phospholipase A2-like proteins revealed by complexation with the inhibitor suramin. Acta Crystallogr D Biol Crystallogr. 2015 Oct;71(Pt 10):2066-78. doi:, 10.1107/S1399004715014443. Epub 2015 Sep 26. PMID:26457430 doi:http://dx.doi.org/10.1107/S1399004715014443

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