Vm24 Scorpion Toxin: Difference between revisions

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Vm24 is a single chain protein consisting of 36 amino acids. It has a molecular weight of 3,873 daltons. It consists of a three strand (S1,S2,S3) anti-parallel <scene name='84/842913/Labeled_beta_strands/1'>beta sheet</scene> and one single turn <scene name='84/842913/Aplha/1'>alpha helix</scene> with <scene name='84/842913/All_disulfides/1'>four disulfide bonds</scene> holding the chain together.  
Vm24 is a single chain protein consisting of 36 amino acids. It has a molecular weight of 3,873 daltons. It consists of a three strand (S1,S2,S3) anti-parallel <scene name='84/842913/Labeled_beta_strands/1'>beta sheet</scene> and one single turn <scene name='84/842913/Aplha/1'>alpha helix</scene> with <scene name='84/842913/All_disulfides/1'>four disulfide bonds</scene> holding the chain together.  
The disulfides exist between <scene name='84/842913/Ssbond_6-26/1'>Cys6 and Cys26</scene>, <scene name='84/842913/Ssbonds_12-31/1'>Cys12 and Cys31</scene>, <scene name='84/842913/Ssbonds_16-33/1'>Cys16 and Cys33</scene>, and <scene name='84/842913/Ssbonds_21-36/1'>Cys21 and Cys36</scene>. The disulfide bonds between <scene name='84/842913/Ssbonds_12-31/1'>Cys12 and Cys31</scene> and <scene name='84/842913/Ssbonds_16-33/1'>Cys16 and Cys33</scene> <scene name='84/842913/Helix_bound/1'>connect the alpha helix</scene> with the C-terminal strand of the β-sheet. The disulfide bridge between <scene name='84/842913/Ssbond_6-26/1'>Cys6 and Cys26</scene> connects the <scene name='84/842913/S1-s2/1'>end of S1 with the end of S2.</scene> The abundant disulfides in this protein are highly important in conferring it's unusual, strained conformation [https://pubmed-ncbi-nlm-nih-gov.ezproxy.uvm.edu/22540187/?from_single_result=Structure%2C+function%2C+and+chemical+synthesis+of+Vaejovis+mexicanus+peptide+24%3A+a+novel+potent+blocker+of+Kv1.3+potassium+channels+of+human+T+lymphocytes.&expanded_search_query=Structure%2C+function%2C+and+chemical+synthesis+of+Vaejovis+mexicanus+peptide+24%3A+a+novel+potent+blocker+of+Kv1.3+potassium+channels+of+human+T+lymphocytes.].   
The disulfides exist between <scene name='84/842913/Ssbond_6-26/1'>Cys6 and Cys26</scene>, <scene name='84/842913/Ssbonds_12-31/1'>Cys12 and Cys31</scene>, <scene name='84/842913/Ssbonds_16-33/1'>Cys16 and Cys33</scene>, and <scene name='84/842913/Ssbonds_21-36/1'>Cys21 and Cys36</scene>. The disulfide bonds between <scene name='84/842913/Ssbonds_12-31/1'>Cys12 and Cys31</scene> and <scene name='84/842913/Ssbonds_16-33/1'>Cys16 and Cys33</scene> <scene name='84/842913/Helix_bound/1'>connect the alpha helix</scene> with the C-terminal strand of the β-sheet. The disulfide bridge between <scene name='84/842913/Ssbond_6-26/1'>Cys6 and Cys26</scene> connects the <scene name='84/842913/S1-s2/1'>end of S1 with the end of S2.</scene> The abundant disulfides in this protein are highly important in conferring it's unusual, strained conformation [https://pubmed-ncbi-nlm-nih-gov.ezproxy.uvm.edu/22540187/?from_single_result=Structure%2C+function%2C+and+chemical+synthesis+of+Vaejovis+mexicanus+peptide+24%3A+a+novel+potent+blocker+of+Kv1.3+potassium+channels+of+human+T+lymphocytes.&expanded_search_query=Structure%2C+function%2C+and+chemical+synthesis+of+Vaejovis+mexicanus+peptide+24%3A+a+novel+potent+blocker+of+Kv1.3+potassium+channels+of+human+T+lymphocytes.].   
Positions <scene name='84/842913/Resi_7-9/1'>7-9</scene> and <scene name='84/842913/Resi_17-20/1'>17-20</scene> are not well defined because they have a reduced number of Nuclear Overhauser effects NOEs [https://pubmed-ncbi-nlm-nih-gov.ezproxy.uvm.edu/22540187/?from_single_result=Structure%2C+function%2C+and+chemical+synthesis+of+Vaejovis+mexicanus+peptide+24%3A+a+novel+potent+blocker+of+Kv1.3+potassium+channels+of+human+T+lymphocytes.&expanded_search_query=Structure%2C+function%2C+and+chemical+synthesis+of+Vaejovis+mexicanus+peptide+24%3A+a+novel+potent+blocker+of+Kv1.3+potassium+channels+of+human+T+lymphocytes.] All <scene name='84/842913/All_disulfides/2'>cysteines</scene> and <scene name='84/842913/Ile4/1'>Ile4</scene> are buried entirely, but all other residues are exposed. <scene name='84/842913/Tyr35/1'>Tyr35</scene> and <scene name='84/842913/Cys36/1'>Cys36</scene> are in a very flexible region, which is interesting because they are adjacent to a disulfide bridge.
Positions <scene name='84/842913/Resi_7-9/1'>7-9</scene> and <scene name='84/842913/Resi_17-20/1'>17-20</scene> are not well defined because they have a reduced number of Nuclear Overhauser effects NOEs [https://pubmed-ncbi-nlm-nih-gov.ezproxy.uvm.edu/22540187/?from_single_result=Structure%2C+function%2C+and+chemical+synthesis+of+Vaejovis+mexicanus+peptide+24%3A+a+novel+potent+blocker+of+Kv1.3+potassium+channels+of+human+T+lymphocytes.&expanded_search_query=Structure%2C+function%2C+and+chemical+synthesis+of+Vaejovis+mexicanus+peptide+24%3A+a+novel+potent+blocker+of+Kv1.3+potassium+channels+of+human+T+lymphocytes.] All <scene name='84/842913/All_disulfides/2'>cysteines</scene> and <scene name='84/842913/Ile4/1'>Ile4</scene> are buried entirely, but all other residues are exposed. <scene name='84/842913/Tyr35/1'>Tyr35</scene> and <scene name='84/842913/Cys36/1'>Cys36</scene> are in a very flexible region, which is interesting because they are adjacent to a <scene name='84/842913/Ssbonds_21-36/1'>disulfide bridge</scene>.
==Function==
==Function==
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