Vm24 Scorpion Toxin
From Proteopedia
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Gurolla G.B et al [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.] isolated the peptide components of ''Vaejovis mexicanus smithi'' venom using high-performance liquid chromatography. Over 200 components were identified. The structure of Vm24 was determined by solution NMR spectroscopy, and it was sequenced via trypsin digestion. The a synthetic Vm24 gene was created and artificially translated to produce the synthetic Vm24 toxin displayed. | Gurolla G.B et al [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.] isolated the peptide components of ''Vaejovis mexicanus smithi'' venom using high-performance liquid chromatography. Over 200 components were identified. The structure of Vm24 was determined by solution NMR spectroscopy, and it was sequenced via trypsin digestion. The a synthetic Vm24 gene was created and artificially translated to produce the synthetic Vm24 toxin displayed. | ||
==General Structure== | ==General Structure== | ||
| - | 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 anti-parallel <scene name='84/842913/Beta/2'>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 Cys21 and Cys36 | + | 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 anti-parallel <scene name='84/842913/Beta/2'>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>. |
Revision as of 15:10, 26 April 2020
Introduction
Vm24 synthetic scorpion toxin is a peptide toxin isolated from Vaejovis mexicanus scorpion venom. It is a potent inhibitor of Kv1.3 potassium channels of human T lymphocytes. Its high affinity and specificity for human lymphocytes makes it a candidate for the treatment of several autoimmune disorders.
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Protein Source
Gurolla G.B et al [1] isolated the peptide components of Vaejovis mexicanus smithi venom using high-performance liquid chromatography. Over 200 components were identified. The structure of Vm24 was determined by solution NMR spectroscopy, and it was sequenced via trypsin digestion. The a synthetic Vm24 gene was created and artificially translated to produce the synthetic Vm24 toxin displayed.
General Structure
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 anti-parallel and one single turn with holding the chain together. The disulfides exist between , , , and .
