The Structures and Evolution of Snake Toxins of the Three-Finger Folding Type

  • Dominique Housset
  • Juan C. Fontecilla-Camps
Part of the Molecular Biology Intelligence Unit book series (MBIU)

Abstract

Because of their impact on human health, snake venoms have been generally the subject of a great deal of attention and several recent reviews describe the properties of their components.1–3 Many of these have enzymatic activity and are either related to digestive proteins such as phospholipases, proteases and nucleases4 or to trypsin inhibitor polypeptides such as the dendrotoxins.5 This has led to the hypothesis that the venom glands of snakes may have been shaped after the pancreas, secreting at first enzymes that later turned into toxic substances.4 The most studied toxins are those found in Elapidae and Hydrophidae snake venoms and several hundred amino acid sequences as well as tens of three-dimensional structures are currently known. One of the best characterized group is the so-called three-finger snake toxins. These proteins, with molecular weights close to 7,000 Da, share a three-dimensional fold first described for erabutoxin b.6,7 The best known members of this group are the short (59–62 amino acids, 4 disulfide bridges), and the long (66–80 amino acids, 4 or 5 disulfide bridges) α-neurotoxins. These proteins bind to the acetylcholine receptor located on the post-synaptic membrane thereby blocking the transformation of the chemical signal transmitted by acetylcholine into a depolarizing one.1 All Elapidae and Hydrophidae venoms seem to contain long neurotoxins and most of them have short neurotoxins (Table 14.1). Other three-finger molecules, devoid of post-synaptic neurotoxic activity, have been purified from cobras and mambas.8–12

Keywords

Crystallization Toxicity Sulfide Lipase Cysteine 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1996

Authors and Affiliations

  • Dominique Housset
  • Juan C. Fontecilla-Camps

There are no affiliations available

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