The venoms of Viperidae and Crotalidae snakes are a rich source of proteins
with activity against various factors involved in coagulation and fibrinol
ysis. These proteins are very specific for their molecular targets, resista
nt to physiological inhibitors and stable in vitro and in vivo. They have t
herefore proved to be useful for diagnostic tests. Based on sequence simila
rities, these snake venom proteins have been classified into various famili
es, such as serine: proteinases, metalloproteinases, C-type lectins, disint
egrins and phospholipases A(2). The various members of a given family, alth
ough structurally similar, act selectively on different blood coagulation f
actors. This opens up the possibility of characterizing the structural elem
ents involved in target molecule recognition. Thus, snake venom proteins pr
ovide excellent models for studies of structure-function relationships. (C)
2000 Societe francaise de biochimie et biologie moleculaire / Editions sci
entifiques et medicales Elsevier SAS.