Study on the binding interaction of three-finger toxins from cobras and mangrove catsnake toward nicotinic acetylcholine receptors: a computational approach
Introduction: Snake venom is a combination of various proteins and peptides that cause diverse biological effects in multiple organ systems. Toxins from three-finger toxin family are the mains toxins in elapid venom. Although these toxins share similarities in their structure, they are known to cau...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | en |
| Published: |
IIUM Press
2022
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| Subjects: | |
| Online Access: | http://irep.iium.edu.my/99407/2/99407_Study%20on%20the%20binding%20interaction%20of%20three-finger%20toxins.pdf http://irep.iium.edu.my/99407/ https://journals.iium.edu.my/ktn/index.php/jp/article/view/171/72 https://doi.org/10.31436/jop.v2i2.171 |
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| Summary: | Introduction: Snake venom is a combination of various proteins and peptides that cause diverse biological effects in multiple organ systems. Toxins from three-finger toxin family are the mains toxins in elapid venom. Although these toxins share similarities in their structure, they are known
to cause a myriad of toxic actions such as neurotoxicity, cardiotoxicity, and cytotoxicity. Unfortunately, many of these toxins are not fully pharmacologically characterized, especially on their binding affinity and selectivity towards receptors and their effects to different organ systems.
Method: This work compared the binding properties of selected three-finger toxins (3FTxs) from cobras (Naja sumatrana and Naja kaouthia) and mangrove catsnake (Boiga dendrophila) towards human and bird nicotinic acetylcholine receptors (α3β2, α4β2, α7) using computational approaches.
The sequence of the selected toxins were obtained from public database e.g UniProt and NCBI. The structure of the toxins without deposited structure were modelled using homology modelling.
Results: The results show that all toxins bind to the orthosteric site, which is located outside the extracellular domain of α subunit for all receptors in both species. Interaction between receptors and toxins occurs by the formation of hydrogen bond, ionic bond, and hydrophobic contact with
important residues involved in their binding pocket.
Conclusion: Based on the data, the toxins showed different binding affinities towards nicotinic acetylcholine receptors in different species. The differences could have a significant impact on the functional characterization of venom caused by these toxins and toxins with nearly similar sequences. |
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