Please use this identifier to cite or link to this item: https://doi.org/10.1046/j.1440-1681.2002.03725.x
Title: Molecular moulds with multiple missions: Functional sites in three-finger toxins
Authors: Kini, R.M. 
Keywords: Calciseptine
Cardiotoxin
Cytotoxin
Fasciculin
Functional site
Muscarinic toxin
Post-synaptic neurotoxin
Protein-protein interaction
Snake venom
Toxin evolution
Issue Date: 2002
Citation: Kini, R.M. (2002). Molecular moulds with multiple missions: Functional sites in three-finger toxins. Clinical and Experimental Pharmacology and Physiology 29 (9) : 815-822. ScholarBank@NUS Repository. https://doi.org/10.1046/j.1440-1681.2002.03725.x
Abstract: 1. Snake venoms are complex mixtures of pharmacologically active peptides and proteins. 2. These protein toxins belong to a small number of superfamilies of proteins. The present review describes structure-function relationships of three-finger toxins. 3. All toxins share a common structure of three β-stranded loops extending from a central core. However, they bind to different receptors/acceptors and exhibit a wide variety of biological effects. 4. Thus, the structure-function relationships of this group of toxins are complicated and challenging. 5. Studies have shown that the functional sites in these 'sibling' toxins are located on various segments of the molecular surface.
Source Title: Clinical and Experimental Pharmacology and Physiology
URI: http://scholarbank.nus.edu.sg/handle/10635/101146
ISSN: 03051870
DOI: 10.1046/j.1440-1681.2002.03725.x
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