Sandbox Reserved 932: Difference between revisions

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Denmotoxin is a monomeric protein comprising of 77 amino acid residues. Denmotoxin consists of <scene name='57/579702/Three_fingers/1'>three polypeptide loops</scene> (fig. 2) protruding from the <scene name='57/579702/3ftx_beta_strands/2'>globular core</scene>; this structure is typical for 3FTXs. The globular core consists of a triple stranded anti-parallel β-sheet; two of the β-strands in this structure connect to the second loop (<scene name='57/579702/The_central_loop/1'>central loop</scene>) and one β-strand connects to the third loop. There are two highly <scene name='57/579702/Flexible_regions/2'>flexible regions</scene> on the protein: one at the tip of the central loop and one at the 3 first residues of the N-terminus; the expected <scene name='57/579702/Active_site/1'>active site</scene> of denmotoxin is at the tip of the <scene name='57/579702/The_central_loop/1'>central loop</scene>. <ref name=Pawlak/>

There are 10 structurally important cysteine-residues in denmotoxin which form five stabilizing <scene name='57/579702/Disulphides/3'>disulphide bonds</scene>. Four of these disulphide bonds, which are found in all 3FTXs are located at the central core and the <scene name='57/579702/Fifth_disulphide/1'>fifth additional bond</scene>is found at the tip of the first loop. The cysteine residues of all 3FTXs are highly conserved, whereas the other residues within the sequence express high variability. Denmotoxin possesses most of the conserved residues invariant among 3FTXs which have been shown to be important for the proper folding of and structure of protein. The presence of these structurally important residues result in the characteristic three finger fold of the toxin (e.g. Gly52, Pro58). <ref name=Pawlak/>

There are 10 structurally important cysteine-residues in denmotoxin which form five stabilizing <scene name='57/579702/Disulphides/3'>disulphide bonds</scene>. Four of these disulphide bonds, which are found in all 3FTXs are located at the central core and the <scene name='57/579702/Fifth_disulphide/1'>fifth additional bond</scene> is found at the tip of the first loop. The cysteine residues of all 3FTXs are highly conserved, whereas the other residues within the sequence express high variability. Denmotoxin possesses most of the conserved residues invariant among 3FTXs which have been shown to be important for the proper folding of and structure of protein. The presence of these structurally important residues result in the characteristic three finger fold of the toxin (e.g. Gly52, Pro58). <ref name=Pawlak/>

Multiple sequence alignment of denmotoxin reveals that the venom belongs to the family of non-conventional 3FTXs. All non-conventional 3FTXs have an additional disulphide bond. Denmotoxin has 7 additional amino acid residues in its N-terminal when compared to other 3FTXs; the N-terminus is also blocked by a pyroglutamic acid residue. This unusually long N-terminus is unstructured and is hypothesized to gyrate above the core of the protein. Another unique feature of denmotoxin is the twist at the tip of the central loop originating from a kink in a proline residue (Pro40). At the central loop, the charge is also negative; an arginine residue has been replaced with an aspartic acid, which is unusual for the proteins of the family. <ref name=Pawlak/>

Multiple sequence alignment of denmotoxin reveals that the venom belongs to the family of non-conventional 3FTXs. All non-conventional 3FTXs have an additional disulphide bond. Denmotoxin has 7 additional amino acid residues in its N-terminal when compared to other 3FTXs; the N-terminus is also blocked by a pyroglutamic acid residue. This unusually long N-terminus is unstructured and is hypothesized to gyrate above the core of the protein. Another unique feature of denmotoxin is the twist at the tip of the central loop originating from a kink in a <scene name='57/579702/Pro40/1'>proline residue</scene> (Pro40). At the central loop, the charge is also negative; an arginine residue has been replaced with an aspartic acid, which is unusual for the proteins of the family. <ref name=Pawlak/>

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 Denmotoxin is a monomeric protein comprising of 77 amino acid residues. Denmotoxin consists of <scene name='57/579702/Three_fingers/1'>three polypeptide loops</scene> (fig. 2) protruding from the <scene name='57/579702/3ftx_beta_strands/2'>globular core</scene>; this structure is typical for 3FTXs. The globular core consists of a triple stranded anti-parallel β-sheet; two of the β-strands in this structure connect to the second loop (<scene name='57/579702/The_central_loop/1'>central loop</scene>) and one β-strand connects to the third loop. There are two highly <scene name='57/579702/Flexible_regions/2'>flexible regions</scene> on the protein: one at the tip of the central loop and one at the 3 first residues of the N-terminus; the expected <scene name='57/579702/Active_site/1'>active site</scene> of denmotoxin is at the tip of the <scene name='57/579702/The_central_loop/1'>central loop</scene>. <ref name=Pawlak/>
-There are 10 structurally important cysteine-residues in denmotoxin which form five stabilizing <scene name='57/579702/Disulphides/3'>disulphide bonds</scene>. Four of these disulphide bonds, which are found in all 3FTXs are located at the central core and the <scene name='57/579702/Fifth_disulphide/1'>fifth additional bond</scene>is found at the tip of the first loop. The cysteine residues of all 3FTXs are highly conserved, whereas the other residues within the sequence express high variability. Denmotoxin possesses most of the conserved residues invariant among 3FTXs which have been shown to be important for the proper folding of and structure of protein. The presence of these structurally important residues result in the characteristic three finger fold of the toxin (e.g. Gly52, Pro58). <ref name=Pawlak/>
+There are 10 structurally important cysteine-residues in denmotoxin which form five stabilizing <scene name='57/579702/Disulphides/3'>disulphide bonds</scene>. Four of these disulphide bonds, which are found in all 3FTXs are located at the central core and the <scene name='57/579702/Fifth_disulphide/1'>fifth additional bond</scene> is found at the tip of the first loop. The cysteine residues of all 3FTXs are highly conserved, whereas the other residues within the sequence express high variability. Denmotoxin possesses most of the conserved residues invariant among 3FTXs which have been shown to be important for the proper folding of and structure of protein. The presence of these structurally important residues result in the characteristic three finger fold of the toxin (e.g. Gly52, Pro58). <ref name=Pawlak/>
-Multiple sequence alignment of denmotoxin reveals that the venom belongs to the family of non-conventional 3FTXs. All non-conventional 3FTXs have an additional disulphide bond. Denmotoxin has 7 additional amino acid residues in its N-terminal when compared to other 3FTXs; the N-terminus is also blocked by a pyroglutamic acid residue. This unusually long N-terminus is unstructured and is hypothesized to gyrate above the core of the protein. Another unique feature of denmotoxin is the twist at the tip of the central loop originating from a kink in a proline residue (Pro40). At the central loop, the charge is also negative; an arginine residue has been replaced with an aspartic acid, which is unusual for the proteins of the family. <ref name=Pawlak/>
+Multiple sequence alignment of denmotoxin reveals that the venom belongs to the family of non-conventional 3FTXs. All non-conventional 3FTXs have an additional disulphide bond. Denmotoxin has 7 additional amino acid residues in its N-terminal when compared to other 3FTXs; the N-terminus is also blocked by a pyroglutamic acid residue. This unusually long N-terminus is unstructured and is hypothesized to gyrate above the core of the protein. Another unique feature of denmotoxin is the twist at the tip of the central loop originating from a kink in a <scene name='57/579702/Pro40/1'>proline residue</scene> (Pro40). At the central loop, the charge is also negative; an arginine residue has been replaced with an aspartic acid, which is unusual for the proteins of the family. <ref name=Pawlak/>