Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin
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چکیده
منابع مشابه
NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels.
The solution structure of chlorotoxin, a small toxin purified from the venom of the Leiurus quinquestriatus scorpion, has been determined using 2D 1H NMR spectroscopy. Analysis of the NMR data shows that the structure consists of a small three-stranded antiparallel beta-sheet packed against an alpha-helix, thereby adopting the same fold as charybdotoxin and other members of the short scorpion t...
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BACKGROUND The hERG potassium channel can modulate the proliferation of the chronic myelogenous leukemic K562 cells, and its role in the erythroid differentiation of K562 cells still remains unclear. PRINCIPAL FINDINGS The hERG potassium channel blockage by a new 36-residue scorpion toxin BmKKx2, a potent hERG channel blocker with IC50 of 6.7 ± 1.7 nM, enhanced the erythroid differentiation o...
متن کاملBmTx3, a scorpion toxin with two putative functional faces separately active on A-type K+ and HERG currents.
A novel HERG channel blocker was isolated from the venom of the scorpion Buthus martensi Karsch, sequenced and characterized at the pharmacological level after chemical synthesis. According to the determined amino acid sequence, the cDNA and genomic genes were then cloned. The genomic gene consists of two exons interrupted by an intron of 65 bp at position -6 upstream from the mature toxin. The...
متن کاملBeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1.
Peptide toxins with disulfide-stabilized structures have been used as molecular calipers to probe the outer vestibule structure of K channels. We want to apply this approach to the human ether-a-go-go-related gene (HERG) channel, whose outer vestibule is unique in structure and function among voltage-gated K channels. Our focus here is BeKm-1, a HERG-specific peptide toxin that can suppress HER...
متن کاملStructure of an excitatory insect-specific toxin with an analgesic effect on mammals from the scorpion Buthus martensii Karsch.
BmK IT-AP is an excitatory insect-specific beta-toxin with analgesic effect from the Chinese scorpion Buthus martensii Karsch (BmK) and consists of 72 residues cross-linked by four disulfide bridges. The crystal structure of BmK IT-AP has been determined at a resolution of 2.6 A by molecular replacement. Compared with the mammal-selective alpha-toxins consisting of 64 residues from the scorpion...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2003
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(03)00216-3