Sandbox Reserved 932: Difference between revisions

Line 22:

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. <ref name=Dufton/>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.

Denmotoxin shares approximately 30% sequence similarity with other 3FTXs with an exception of exhibiting approximately 50% sequence similarity with another colubrid snake venom α-colubritoxin. Despite the relatively low sequence similarity, denmotoxin possesses all the residues needed to maintain the 3 finger fold. A large part of the sequence similarity between denmotoxin and other 3FTXs is due to the highly conserved disulphides and a number of structurally important residues.

Sandbox Reserved 932: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 15:06, 18 May 2014 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 15:07, 18 May 2014 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
Line 22:		Line 22:


	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. <ref name=Dufton/>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.

	Denmotoxin shares approximately 30% sequence similarity with other 3FTXs with an exception of exhibiting approximately 50% sequence similarity with another colubrid snake venom α-colubritoxin. Despite the relatively low sequence similarity, denmotoxin possesses all the residues needed to maintain the 3 finger fold. A large part of the sequence similarity between denmotoxin and other 3FTXs is due to the highly conserved disulphides and a number of structurally important residues.		Denmotoxin shares approximately 30% sequence similarity with other 3FTXs with an exception of exhibiting approximately 50% sequence similarity with another colubrid snake venom α-colubritoxin. Despite the relatively low sequence similarity, denmotoxin possesses all the residues needed to maintain the 3 finger fold. A large part of the sequence similarity between denmotoxin and other 3FTXs is due to the highly conserved disulphides and a number of structurally important residues.