Sandbox Reserved 932: Difference between revisions
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=== Denmotoxin belongs to a family of non-conventional three-finger toxins === | === Denmotoxin belongs to a family of non-conventional three-finger toxins === | ||
Three-finger toxins (3FTXs) are the most common family of snake venom proteins; these venoms can be found in elapid, colubrid and hydrophiid snakes and include toxins such as α-cobratoxin and α-bungarotoxin. 3FTXs are non-enzymatic proteins which form a structurally conserved superfamily whose members all share a highly conserved structure. The core structure of 3FTXs is formed by three <scene name='57/579702/Three_fingers/1'>three β-stranded polypeptide loops</scene> joined together by four conserved disulphide bridges located in the <scene name='57/579702/3ftx_beta_strands/2'>core</scene> of the protein. Despite the similarities in the structure of different toxins belonging to the family, the 3FTXs from various venoms have a variety of receptors/acceptors and exhibit differential responses in their targets. The members of the family can vary slightly in: the length and type of twists of the tree loops; the length and type of turns of the N and C-terminal tail and the amount of β-sheets in the overall structure. These differences allow for the specificity and toxicity of the proteins to their targets. | Three-finger toxins (3FTXs) are the most common family of snake venom proteins; these venoms can be found in elapid, colubrid and hydrophiid snakes and include toxins such as α-cobratoxin and α-bungarotoxin. 3FTXs are non-enzymatic proteins which form a structurally conserved superfamily whose members all share a highly conserved structure. The core structure of 3FTXs is formed by three <scene name='57/579702/Three_fingers/1'>three β-stranded polypeptide loops</scene> joined together by four conserved disulphide bridges located in the <scene name='57/579702/3ftx_beta_strands/2'>core</scene> of the protein. Despite the similarities in the structure of different toxins belonging to the family, the 3FTXs from various venoms have a variety of receptors/acceptors and exhibit differential responses in their targets. The members of the family can vary slightly in: the length and type of twists of the tree loops; the length and type of turns of the N and C-terminal tail and the amount of β-sheets in the overall structure. These differences allow for the specificity and toxicity of the proteins to their targets. | ||