Non-conventional toxins from Elapid venoms.

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Title Non-conventional toxins from Elapid venoms.
Author Nirthanan, S. Niru; Gopalakrishnakone, P.; Gwee, M. C. E.; Khoo, H. E.; Kini, R. M.
Journal Name Toxicon
Year Published 2003
Place of publication Amsterdam
Publisher Elsevier Science
Abstract Non-conventional toxins constitute a poorly characterized class of three-finger toxins isolated exclusively from Elapidae venoms. These toxins are monomers of 62–68 amino acid residues and contain five disulfide bridges. However, unlike α/κ-neurotoxins and κ-neurotoxins which have the fifth disulfide bridge in their middle loop (loop II), the fifth disulfide bridge in non-conventional toxins is located in loop I (N-terminus loop). Overall, non-conventional toxins share ~28–42% identity with other three-finger toxins including α-neurotoxins, α/κ-neurotoxins and κ-neurotoxins. Recent structural studies have revealed that non-conventional toxins also display the typical three-finger motif. Non-conventional toxins are typically characterized by a lower order of toxicity (LD50~5–80 mg/kg) in contrast to prototype α-neurotoxins (LD50~0.04–0.3 mg/kg) and hence they are also referred to as 'weak toxins'. Further, it is generally assumed that non-conventional toxins target muscle (α2βγδ) receptors with low affinities several orders of magnitude lower than α-neurotoxins and α/κ-neurotoxins. However, it is now known that some non-conventional toxins also antagonize neuronal α7 nicotinic acetylcholine receptors. Hence, non-conventional toxins are not a functionally homogeneous group and other, yet unknown, molecular targets for this class of snake venom toxins may exist. Non-conventional toxins may therefore be a useful source of ligands with novel biological activity targeting the plethora of neuronal nicotinic receptors as well as other physiological processes.
Peer Reviewed Yes
Published Yes
Publisher URI http://www.elsevier.com/wps/find/journaldescription.cws_home/259/description#description
Alternative URI http://dx.doi.org/10.1016/S0041-0101(02)00388-4
Volume 41
Issue Number 4
Page from 397
Page to 407
ISSN 0041-0101
Date Accessioned 2009-07-09
Date Available 2009-12-18T06:34:11Z
Language en_AU
Research Centre Griffith Health Institute
Faculty Griffith Health Faculty
Subject Biochemistry and Cell Biology; Physiology
URI http://hdl.handle.net/10072/27781
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1x

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