Single snake venom often contains multiple isoforms of phospholipase A₂ (PLA₂).  At times, these isoforms exhibit distinct pharmacological activities. Such protein diversity is achieved by gene duplication and accelerated evolution of their exons. By comparing the structures of 127 snake venom PLA₂ enzymes, we showed that mutational hot spots occur on the surface of PLA₂ protein. Natural substitutions occur about 2.6-3.5 times greater in fully exposed residues than in the buried residues. The surface substitutions and the accelerated evolution of exons play a significant role in the evolution of new PLA₂ isoenzymes by altering the target specificity.

 

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