Binding of acidic PLA2 Ba SPII RP4 from Bothrops alternatus snake venom to integrin αvβ3: An in silico study

Abstract

We have previously demonstrated that BaSpIIRP4 (an acidic PLA2 from Bothrops alternatus venom), enhance the endothelial cells (EC) detachment effect of a snake venom metalloproteinase. Considering that the binding of cells to their ligands depends on the interaction between extracellular matrix and integral membrane proteins, this effect may be due to interactions between PLA2 and EC integrins. The integrin alpha-v beta-3 (αvβ3) is commonly expressed in endothelial cells. It has been reported that human PLA2-IIA binds to this integrin with high affinity....