Convulxin  Convulxin is a snake venom toxin found in a tropical rattlesnake known as "Crotalus durissus terrificus". It belongs to the family of hemotoxins, which destroy red blood cells or, as is the case with convulxin, induce blood coagulation. It causes platelet activation in the blood, forming clots and buildup of pressure. Convulxin acts as an agonist to the GPVI receptor, the major signalling receptor for collagen. This can cause the blood stream to burst, or the heart or brain to lose blood, thus resulting in death. It is a tetramer C-type lectin with an oligomeric structure, made up of heterodimeric subunits. Convulxin is part of the snake venom C-type lectin family, a group of hemorrhagic toxins that disrupt body homeostasis. The name describes their similarity in structure to C-type lectins from other animals, proteins that bind calcium to induce various signalling pathways. Proteins of about 130 amino acids in length, C-type lectins contain at least a carbohydrate recognition domain (CRD), which mediates sugar and calcium binding. They are involved in various biological activities, ranging from cell-cell adhesion, serum glycoprotein turnover, to immune responses and cell apoptosis. The toxin was first described in detail in 1969 by two Brazilian researchers from University of Campinas, Júlia Prado-Franceschi and Oswaldo Vital-Brazil. The snake C-type lectin convulxin was reported to activate platelets in a similar way to collagen in the late 1970s, but this was only announced after the discovery of the association with the FcR γ-chain and after it was recognized to mediate activation through GPVI. Now this toxin is widely used to study mamalian platelet receptors. Convulxin is a heterodimer made up of α-(13.9 kDa) and β- (12.6 kDa) subunits, with 38% sequence identity and homologous structures. The subunits are connected by disulfide bridges to form a cyclic, ring-like α4β4 structure . Its function arises from its ability to bind with high affinity to the platelet receptor for collagen, glycoprotein (GP) VI. It is, therefore, an important task to determine the binding site on the heterodimer to the GPVI.