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- Q4930965 subject Q9089708.
- Q4930965 abstract "In molecular biology, the BmKK2 toxins are a family of scorpion toxins. They belong to the scorpion toxin subfamily alpha-KTx 14. They include a novel short-chain peptide from the Asian scorpion Mesobuthus martensii Karsch, a potassium channel blocker composed of 31 amino acid residues. The peptide adopts a classical alpha/beta-scaffold for alpha-KTxs. BmKK2 selectively inhibits the delayed rectifier K+ current, but does not affect the fast transient K+ current.In comparison with typical short-chain scorpion toxins (e.g., CTX and NTX), the alpha helix is shorter and the beta-sheet element is smaller (each strand consists of only two residues). There is an alpha-mode binding between the toxin and the channels. It has a lower activity towards Kv channels and it is predicted that it may prefer a type of SK channel with a narrower entryway as a specific receptor.".
- Q4930965 wikiPageWikiLink Q1319714.
- Q4930965 wikiPageWikiLink Q172847.
- Q4930965 wikiPageWikiLink Q184651.
- Q4930965 wikiPageWikiLink Q19125.
- Q4930965 wikiPageWikiLink Q208467.
- Q4930965 wikiPageWikiLink Q283399.
- Q4930965 wikiPageWikiLink Q283449.
- Q4930965 wikiPageWikiLink Q423778.
- Q4930965 wikiPageWikiLink Q6507061.
- Q4930965 wikiPageWikiLink Q8066.
- Q4930965 wikiPageWikiLink Q9089708.
- Q4930965 comment "In molecular biology, the BmKK2 toxins are a family of scorpion toxins. They belong to the scorpion toxin subfamily alpha-KTx 14. They include a novel short-chain peptide from the Asian scorpion Mesobuthus martensii Karsch, a potassium channel blocker composed of 31 amino acid residues. The peptide adopts a classical alpha/beta-scaffold for alpha-KTxs.".
- Q4930965 label "BmKK2 toxin".