HsTx1: Difference between revisions
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Latest revision as of 18:35, 18 March 2025
HsTx1 is a toxin found in the venom of the scorpion species Heterometrus spinifer. It is a potassium channel blocker, specifically affecting voltage-gated potassium channels.
Structure[edit]
HsTx1 is a 34 amino acid peptide with a molecular weight of approximately 4 kDa. It has a compact structure stabilized by three disulfide bonds. The structure of HsTx1 is similar to other scorpion toxins that affect potassium channels, such as Charybdotoxin and Margatoxin.
Function[edit]
HsTx1 blocks voltage-gated potassium channels, specifically the Kv1.3 and Kv1.2 channels. It does this by binding to the outer vestibule of the channel, preventing potassium ions from passing through. This blockage can lead to prolonged action potentials and increased neuronal excitability.
Clinical significance[edit]
Due to its ability to block Kv1.3 channels, HsTx1 has potential therapeutic applications. Kv1.3 channels are overexpressed in T cells of patients with autoimmune diseases, and blocking these channels can suppress the immune response. Therefore, HsTx1 could potentially be used as a treatment for autoimmune diseases such as rheumatoid arthritis, multiple sclerosis, and type 1 diabetes.
See also[edit]
References[edit]
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