Protein complexes in snake venom |
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| Authors: | R Doley R M Kini |
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| Institution: | (1) Protein Science Laboratory, Department of Biological Sciences, Faculty of Science, National University of Singapore, 10 Kent Ridge Crescent, Singapore, 119260, Singapore;(2) Present address: Department of Molecular Biology and Biotechnology, Tezpur University, Assam, India;(3) Department of Biochemistry, Medical College of Virginia, Virginia Commonwealth University, Richmond, VA, USA |
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| Abstract: | 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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| Keywords: | PLA2 complexes Metalloprotease complexes Dimeric disintegrin Serine protease complexes Covalent and non-covalent three-finger toxin Synergistic three-finger toxin |
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