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Sandbox Reserved 932
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''B. Dendrophila'' monomeric toxin (Denmotoxin) is the primary protein of snake venom used by ''Boiga dendrophila''. This colubrid snake lives in Southest Asian lowland rainforest and mangrove swamps using birds as its primary prey. | ''B. Dendrophila'' monomeric toxin (Denmotoxin) is the primary protein of snake venom used by ''Boiga dendrophila''. This colubrid snake lives in Southest Asian lowland rainforest and mangrove swamps using birds as its primary prey. | ||
| - | One of the most well characterized snake venom protein families is the Three-finger-toxins (3FTX). These proteins have three β-stranded finger-like 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 | + | One of the most well characterized snake venom protein families is the Three-finger-toxins (3FTX). These proteins have three β-stranded finger-like 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. |
How the overall structure looks like? Subunits orientation, chains: the number and relative positions, etc. | How the overall structure looks like? Subunits orientation, chains: the number and relative positions, etc. | ||
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===Structure=== | ===Structure=== | ||
| - | Denmotoxin is a monomeric protein possessing 77 amino acid residues including 10 structurally important cysteines. Multiple sequence alignment of denmotoxin reveals that the venom belongs to the family of non-conventional 3FTXs. Denmotoxins cysteines form <scene name='57/579702/Disulphides/2'>five disulphide bonds</scene> which stabilize the structure. Denmotoxin has 7 additional amino acid residues in its N-terminal when compared to other elapid 3FTXs; the N-terminus is also blocked by a pyroglutamic acid residue. The cysteine residues of all 3FTXs are highly conserved, whereas the other residues within the sequence express high variabilty. The biological function of the pyroglutamic acid residue is currently unknown. There are two highly flexible regions on the protein: one at the tip of the central loop and one at the 3 first residues of the N-terminus. | + | Denmotoxin is a non-covalent monomeric protein possessing 77 amino acid residues including 10 structurally important cysteines. Multiple sequence alignment of denmotoxin reveals that the venom belongs to the family of non-conventional 3FTXs. Denmotoxins cysteines form <scene name='57/579702/Disulphides/2'>five disulphide bonds</scene> which stabilize the structure. Denmotoxin has 7 additional amino acid residues in its N-terminal when compared to other elapid 3FTXs; the N-terminus is also blocked by a pyroglutamic acid residue. The cysteine residues of all 3FTXs are highly conserved, whereas the other residues within the sequence express high variabilty. The biological function of the pyroglutamic acid residue is currently unknown. There are two highly flexible regions on the protein: one at the tip of the central loop and one at the 3 first residues of the N-terminus. |
=== Denmotoxin interacts with acetylcholine-receptors === | === Denmotoxin interacts with acetylcholine-receptors === | ||
Revision as of 10:39, 14 May 2014
| This Sandbox is Reserved from 01/04/2014, through 30/06/2014 for use in the course "510042. Protein structure, function and folding" taught by Prof Adrian Goldman, Tommi Kajander, Taru Meri, Konstantin Kogan and Juho Kellosalo at the University of Helsinki. This reservation includes Sandbox Reserved 923 through Sandbox Reserved 947. |
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Denmotoxin
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