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Sandbox Reserved 932

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===Structure===
===Structure===
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Denmotoxin is a monomeric protein possessing 77 amino acid residues including 10 cysteines. Multiple sequence alignment of denmotoxin reveals that the venom belongs to the family of non-conventional 3FTXs. Compared to conventional 3FTxs denmotoxins has 7 additional amino acids. The calculated mass of the protein is 8507.8 Da. Has <scene name='57/579702/Disulphides/2'>five disulphide bonds</scene>. Belongs to a family of non-conventional 3FTXs (3 finger toxins). 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. 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.
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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. Compared to conventional 3FTXs denmotoxin has 7 additional amino acids in its N-terminus. The calculated mass of the protein is 8507.8 Da. Has <scene name='57/579702/Disulphides/2'>five disulphide bonds</scene>. Belongs to a family of non-conventional 3FTXs (3 finger toxins). 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. 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 ===
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Biochemistry of denmotoxin is unique for its specifity to bird nicotinic acetyl choline receptors. Binding of denmotoxin to chick muscle AcHR (α1βγδ) is a highly irreversible where as interaction with identical subunit assembly in mouse AcHR was reversible. Here a picture of the complex where the toxin is bound to the AChR. The active sites which interact with the receptor.
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Biochemistry of denmotoxin is unique for its specifity to bird nicotinic acetyl choline receptors. Binding of denmotoxin to a chick muscle AcHR (a1ByS) is a highly irreversible when interaction with identical subunit assembly in mouse AcHR was reversible. Here a picture of the complex where the toxin is bound to the AChR. The active sites which interact with the receptor.
===Active site organisation===
===Active site organisation===

Revision as of 10:03, 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

Structure of denmotoxin (PDB entry 2H5F)

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Additional Information

References

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