Vm24 Scorpion Toxin
From Proteopedia
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Gurolla G.B et al ***link*** 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 ***link*** 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/ | + | 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 alpha helix, with four disulfide bonds holding the chain together. The disulfides exist between Cys6 and Cys26, Cys12 and Cys31, Cys12 and Cys33, and Cys21 and Cys36 |
| + | <scene name='84/842913/Beta/2'>Text To Be Displayed</scene> | ||
Revision as of 20:11, 24 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 ***link*** 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 alpha helix, with four disulfide bonds holding the chain together. The disulfides exist between Cys6 and Cys26, Cys12 and Cys31, Cys12 and Cys33, and Cys21 and Cys36
