Snake Venom Metalloproteinases (SVMPs): A structure-function update.

摘要: Abstract Snake venom metalloproteinases (SVMPs) represent a diverse group of multi-domain proteins with several biological activities such as the ability to induce hemorrhage, proteolytic degradation fibrinogen and fibrin, induction apoptosis inhibition platelet aggregation. Due these activities, SVMPs are responsible for many well-known pathological phenotypes in snake envenomations caused particularly by species from Viperidae family Crotalinae subfamily. These have been classified based on their size domain structure into P-I, P-II P-III classes. Comparatively, members P-I possess simplest structures, formed catalytic metalloproteinase only; moderately more complex, having canonical disintegrin addition domain; class structurally varied, comprising metalloproteinase, disintegrin-like, cysteine-rich domains. Proteolytic cleavage, repeated loss presence other ancillary domains structural diversities class. However, studies continue unveil relationship between function proteins. In this review, we recovered evidences literature peculiarities functional classification Venom Metalloproteinases. addition, reflect that exist among each while taking account specific up-to-date class-based activities.