Vm24 Scorpion Toxin: Difference between revisions
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Vm24 is a potent and selective inhibitor of Kv1.3 potassium channels of human T lymphocytes. In vitro, Kv1.3 current is reduced by approximately 2/3 <sub>rds</sub> in the presence of 3pM of Vm24. The synthetic and natural forms of this protein have nearly identical activity, but the synthetic toxin could be slightly more potent. K<sub>d synthetic</sub> =0.5pM and K<sub>d native</sub> = 2.9 pM, but this difference is mostly attributed to measurement difficulties at low concentrations [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.]. At a higher concentration of 100pM, both the synthetic and native peptides reduce Kv1.3 current by 90%. | Vm24 is a potent and selective inhibitor of Kv1.3 potassium channels of human T lymphocytes. In vitro, Kv1.3 current is reduced by approximately 2/3 <sub>rds</sub> in the presence of 3pM of Vm24. The synthetic and natural forms of this protein have nearly identical activity, but the synthetic toxin could be slightly more potent. K<sub>d synthetic</sub> =0.5pM and K<sub>d native</sub> = 2.9 pM, but this difference is mostly attributed to measurement difficulties at low concentrations [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.]. At a higher concentration of 100pM, both the synthetic and native peptides reduce Kv1.3 current by 90%. | ||
==Phylogeny== | ==Phylogeny== | ||
Vm24 is a member of the short scorpion toxin superfamily, potassium channel inhibitor family, and | Vm24 is a member of the short scorpion toxin superfamily[https://www.uniprot.org/uniprot/?query=family%3A%22short+scorpion+toxin+superfamily%22&sort=score], potassium channel inhibitor family[https://www.uniprot.org/uniprot/?query=family:%22short+scorpion+toxin+superfamily.+Potassium+channel+inhibitor+family%22&sort=score]. Vm24 appears as a sister clade to the α-KTx subfamilies 6 and 7, and is thus proposed as a novel new subfamily α-KTx 23.1[https://www.uniprot.org/uniprot/?query=family:%22short+scorpion+toxin+superfamily.+Potassium+channel+inhibitor+family.+Alpha-KTx+23+subfamily%22&sort=score]. The alpha-KTx 23 subfamily contains proteins with the CSalpha/beta fold, which comprises one or two short alpha helices connected to anti-parallel beta-sheets stabilized by three or four disulfide bonds. | ||
