Sandbox Reserved 932: Difference between revisions

B. Dendrophila monomeric toxin (Denmotoxin) is the primary protein of snake venom used by ''Boiga dendrophila'' (fig. 1). This colubrid snake lives in Southest Asian lowland rainforest and mangrove swamps using birds as its primary prey. It belongs to one of the most well characterized snake venom protein families is the Three-finger-toxins (3FTX). These proteins consist of three β-stranded finger-like polypeptide loops stabilized by four disulphide bridges on the surface of a globular core. In non-convential 3TFXs a fifth disulphide bridge can be present as is the case in Denmotoxin. The crystal structure of denmotoxin was solved in a resolution of 1.9Å by molecular replacement method. <ref name=Dufton>Dufton M.J. & Hider R.C., [http://www.ncbi.nlm.nih.gov/pubmed/3277206 "Structure and pharmacology of elapid cytotoxins"], ''Pharmacol Ther. 1988;36(1):1-40'', 1988. Retrieved May 19, 2014.</ref><ref name=Endo>Endo T. & Tamiya N., Structure-function relationship of postsynaptic neurotoxins from snake venoms, ''Snake Toxins, pp. 165-222.'', 1991. Retrieved May 19, 2014.</ref>

Denmotoxin binds specifically to bird muscle nicotinic acetylcholine receptors preventing their normal function in signal transduction. This taxon specifity is reached by unique structural differences to other 3FTXs such as changes in the suggested binding loop of the protein. <ref name=Pawlak>Pawlak J. ''et al.'', [http://www.ncbi.nlm.nih.gov/pubmed/16864572 "Denmotoxin, a Three-finger Toxin from the Colubrid Snake Boiga dendrophila (Mangrove Catsnake) with Bird-specific Activity"], ''The Journal of Biological Chemistry: 281: 29030-29041'', September 29, 2006. Retrieved May 19, 2014.</ref><ref name=Pawlak/>