Please use this identifier to cite or link to this item:
|Title:||Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets||Authors:||Kini, R.M.
Dimeric three finger toxin
|Issue Date:||Nov-2010||Citation:||Kini, R.M., Doley, R. (2010-11). Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets. Toxicon 56 (6) : 855-867. ScholarBank@NUS Repository. https://doi.org/10.1016/j.toxicon.2010.07.010||Abstract:||Snake venoms are complex mixtures of pharmacologically active peptides and proteins. These protein toxins belong to a small number of superfamilies of proteins. Three-finger toxins belong to a superfamily of non-enzymatic proteins found in all families of snakes. They have a common structure of three β-stranded loops extending from a central core containing all four conserved disulphide bonds. Despite the common scaffold, they bind to different receptors/acceptors and exhibit a wide variety of biological effects. Thus, the structure-function relationships of this group of toxins are complicated and challenging. Studies have shown that the functional sites in these 'sibling' toxins are located on various segments of the molecular surface. Targeting to a wide variety of receptors and ion channels and hence distinct functions in this group of mini proteins is achieved through a combination of accelerated rate of exchange of segments as well as point mutations in exons. In this review, we describe the structural and functional diversity, structure-function relationships and evolution of this group of snake venom toxins. © 2010 Elsevier Ltd.||Source Title:||Toxicon||URI:||http://scholarbank.nus.edu.sg/handle/10635/102550||ISSN:||00410101||DOI:||10.1016/j.toxicon.2010.07.010|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.