Search for a "toxic site" in snake venom phospholipases A2.
Secondary structure predictions on nine snake venom phospholipases A2 by the Chou and Fasman and Cid et al. prediction methods, have led to the location of two possible "toxic sites", responsible for the neurotoxic and myotoxic action of the basic snake venom PLA2, respectively. The accessibility to the neurotoxic site is blocked by the presence of a small helical structure (helix D in the bovine PLA2). The role of lysine residues is found to be decisive in the venom's toxicity.
Arriagada
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Departamento de Biología Molecular, Facultad de Ciencias Biológicas y de Recursos Naturales, Universidad de Concepción, Chile.
Cid
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H
D000595:Amino Acid Sequence; D000818:Animals; D008239:Lysine; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000633:toxicity*; D010740:Phospholipases / Q000633:toxicity*; D010741:Phospholipases A / Q000378:metabolism / Q000633:toxicity*; D054467:Phospholipases A2; D011487:Protein Conformation; D012910:Snake Venoms / Q000032:analysis* / Q000378:metabolism / Q000633:toxicity*
D009498:Neurotoxins; D012910:Snake Venoms; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D008239:Lysine