ABSTRACT
Snakes and their venoms have both terrified and fascinated humans throughout history and have also been used as drugs and antidotes. Historically, venoms were considered to be composed of very different types of molecules or toxins, but biochemical and crystallographic experiments have shown that they consist of peptides and proteins that are chemically and structurally homologous to the snake’s own tissue counterparts. Three-dimensional structures have provided the basis for understanding the determinants of toxicity, specificity and catalysis that promote or inhibit diverse biological functions such as pain, inflammation, coagulation, neurotoxicity and antifungal activities. The crystallographic techniques and the structural results obtained over the last 80 years indicate the extensive progress that has been made, and venom proteins and peptides often serve as model systems for the development of drugs.
