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Title: Protein complexes in snake venom
Authors: Doley, R. 
Kini, R.M. 
Keywords: Covalent and non-covalent three-finger toxin
Dimeric disintegrin
Metalloprotease complexes
PLA2 complexes
Serine protease complexes
Synergistic three-finger toxin
Issue Date: Sep-2009
Citation: Doley, R., Kini, R.M. (2009-09). Protein complexes in snake venom. Cellular and Molecular Life Sciences 66 (17) : 2851-2871. ScholarBank@NUS Repository.
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. © 2009 Birkhäuser Verlag.
Source Title: Cellular and Molecular Life Sciences
ISSN: 1420682X
DOI: 10.1007/s00018-009-0050-2
Appears in Collections:Staff Publications

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