Snaclecs (snake C-type lectins) that inhibit or activate platelets by binding to receptors.
More than 300 known species of venomous snakes are classified into five families, Hydrophidae, Elapidae, Viperidae, Crotalidae and Colubidae. Venom proteins have also been demonstrated recently in other snakes and some lizards (Fry et al., 2006). Venom components that affect hemostasis are most generally found in Viperidae, and Crotalidae snakes but the others often contain some as well. This review concentrates on structural and functional properties of venom components of the C-type lectin related class (now named snaclecs) that inhibit or activate platelets by binding to receptors.
Clemetson
Kenneth J
KJ
Department of Haematology, University of Berne, Inselspital, CH-3010 Berne, Switzerland. Clemetson@tki.unibe.ch
D000818:Animals; D001665:Binding Sites; D001792:Blood Platelets / Q000187:drug effects*; D038982:Integrin alpha2beta1 / Q000378:metabolism; D037181:Lectins, C-Type / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D008562:Membrane Glycoproteins / Q000378:metabolism; D008958:Models, Molecular; D015539:Platelet Activation / Q000187:drug effects*; D010980:Platelet Membrane Glycoproteins / Q000378:metabolism; D017434:Protein Structure, Tertiary; D012910:Snake Venoms / Q000737:chemistry / Q000633:toxicity*
D038982:Integrin alpha2beta1; D037181:Lectins, C-Type; D008562:Membrane Glycoproteins; D010980:Platelet Membrane Glycoproteins; D012910:Snake Venoms; C098341:platelet membrane glycoprotein VI