Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 66, Issue 17, Pages 2851-2871Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-009-0050-2
Keywords
PLA(2) complexes; Metalloprotease complexes; Dimeric disintegrin; Serine protease complexes; Covalent and non-covalent three-finger toxin; Synergistic three-finger toxin
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Funding
- Biomedical Research Council (BMRC) of Singapore
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Snake venom contains mixture of bioactive proteins and polypeptides. Most of these proteins and polypeptides exist as monomers, but some of them form complexes in the venom. These complexes exhibit much higher levels of pharmacological activity compared to individual components and play an important role in pathophysiological effects during envenomation. They are formed through covalent and/or non-covalent interactions. The subunits of the complexes are either identical (homodimers) or dissimilar (heterodimers; in some cases subunits belong to different families of proteins). The formation of complexes, at times, eliminates the non-specific binding and enhances the binding to the target molecule. On several occasions, it also leads to recognition of new targets as protein-protein interaction in complexes exposes the critical amino acid residues buried in the monomers. Here, we describe the structure and function of various protein complexes of snake venoms and their role in snake venom toxicity.
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