Probing the structure, function, dynamics, and folding of snake venom cardiotoxins

Snake cardiotoxins are small molecular weight (6.5 - 7.0 kDa), highly basic (pI > 10), all beta-sheet proteins. This class of toxins exhibit a wide array of interesting biological properties. The secondary structural elements in these proteins include antiparallel double and triple stranded beta-sheets. Three-dimensional structures of cardiotoxins consistently reveal a cluster of cationic residues encircling, well organized hydrophobic patches. Such an asymmetric distribution of the positively charged and the non-polar residues is believed to important cytolytic activity exhibited by the class of toxins. The aim of this comprehensive review is to summarize and critically evaluate the progress made in research on the structure, function, dynamics and folding of snake venom cardiotoxins.