Snake venom proteins acting on hemostasis.
The venoms of Viperidae and Crotalidae snakes are a rich source of proteins with activity against various factors involved in coagulation and fibrinolysis. These proteins are very specific for their molecular targets, resistant to physiological inhibitors and stable in vitro and in vivo. They have therefore proved to be useful for diagnostic tests. Based on sequence similarities, these snake venom proteins have been classified into various families, such as serine proteinases, metalloproteinases, C-type lectins, disintegrins and phospholipases A(2). The various members of a given family, although structurally similar, act selectively on different blood coagulation factors. This opens up the possibility of characterizing the structural elements involved in target molecule recognition. Thus, snake venom proteins provide excellent models for studies of structure-function relationships.
Braud
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Unité des Venins, Institut Pasteur, 25, rue du Docteur-Roux, 75015, Paris, France.
Bon
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Wisner
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D000595:Amino Acid Sequence; D000818:Animals; D019483:Disintegrins / Q000494:pharmacology*; D006487:Hemostasis / Q000187:drug effects*; D006801:Humans; D037102:Lectins / Q000494:pharmacology*; D008666:Metalloendopeptidases / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010741:Phospholipases A / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000494:pharmacology*; D012910:Snake Venoms / Q000201:enzymology*; D013329:Structure-Activity Relationship
D019483:Disintegrins; D037102:Lectins; D012910:Snake Venoms; D010741:Phospholipases A; D012697:Serine Endopeptidases; D008666:Metalloendopeptidases