CARDIOTOXIN FROM TAIWAN COBRA (NAJA NAJA ATRA): STRUCTURE, DYNAMICS, INTERACTION AND PROTEIN FOLDING

Abstract

Snake venom cardiotoxins, small molecular weight all β-sheet proteins, exhibit a broad spectrum of biological activities. The secondary structure elements in cardiotoxins include an antiparallel triple and a double stranded β-sheet. Basically, cardiotoxins are ‘three-finger’ shaped proteins with three loops projecting from a globular head. The three dimensional structures of these toxins reveal a unique asymmetric distribution of the hydrophobic and hydrophilic amino acids. Irrespective of 90% homology in the amino acid sequence that exists among these cardiotoxin isoforms, each differ in lethal potency. However, to date, there is no clear structure-function correlation(s) available for snake venom cardiotoxins. In this mini review, we provide an overview of our understanding and knowledge of the structure functional relationships of cardiotoxins from the Tawian cobra, Naja naja atra with critical evaluation on the recent progress in research on the structure, dynamics, interaction and folding aspects of snake cardiotoxins.

Keywords: :

• Cardiotoxin III
• Three dimensional Structure
• Protein folding
• Backbone dynamics