Solution structure of BmP01 from the venom of scorpion Buthus martensii Karsch.

@article{Wu2000SolutionSO,
  title={Solution structure of BmP01 from the venom of scorpion Buthus martensii Karsch.},
  author={G. Wu and Y. Li and D. Wei and F. He and S. Jiang and Guoyuan Hu and Houming Wu},
  journal={Biochemical and biophysical research communications},
  year={2000},
  volume={276 3},
  pages={
          1148-54
        }
}
  • G. Wu, Y. Li, +4 authors Houming Wu
  • Published 2000
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
    • From the venom of scorpion Buthus martensii Karsch,a short peptide (BmP01, 29 amino acid residues) was isolated and characterized as previously reported (Lebren, R. R., et al. (1997) Eur. J. Biochem. 245, 457-464). It was shown to reduce 33% outward K(+) channel (hippocampal neurons) currents at 10 microM. The solution structure of BmP01 was determined by 2D (1)H NMR spectroscopy. The NOEs, coupling constants, and H-D exchange obtained from NMR spectroscopy were used in structural calculations… CONTINUE READING
    View on PubMed
    doi.org
    18 Citations
    Background Citations
    4

    Topics from this paper

    Explore Further: Topics Discussed in This Paper

    18 Citations
    Citation Type

    Citation Type

    Solution structure of BmP08, a novel short-chain scorpion toxin from Buthus martensi Karsch.
    • X. Chen, Y. Li, +4 authors Houming Wu
    • Chemistry, Medicine
    • Biochemical and biophysical research communications
    • 2005
    • 2
    The solution structure of BmTx3B, a member of the scorpion toxin subfamily α‐KTx 16
    • 13
    1H-NMR signal assignments and secondary structure analysis of martentoxin
    • Y-H Wang, Z-Y Cao, +5 authors D-Q Yu
    • Chemistry, Medicine
    • Journal of Asian natural products research
    • 2006
    • 3
    Solution structure of BmKK2, a new potassium channel blocker from the venom of chinese scorpion Buthus martensi Karsch
    • 11
    An overview of toxins and genes from the venom of the Asian scorpion Buthus martensi Karsch.
    • 247
    BmKK4, a novel toxin from the venom of Asian scorpion Buthus martensi Karsch, inhibits potassium currents in rat hippocampal neurons in vitro.
    • 7
    NMR solution structure of BmK-betaIT, an excitatory scorpion beta-toxin without a 'hot spot' at the relevant position.
    • 8
    Purification and pharmacological characterization of BmKK2 (alpha-KTx 14.2), a novel potassium channel-blocking peptide, from the venom of Asian scorpion Buthus martensi Karsch.
    • 5
    BmTx3B, a novel scorpion toxin from Buthus martensi Karsch, inhibits delayed rectifier potassium current in rat hippocampal neurons.
    • 6
    • PDF
    Molecular Diversity and Functional Evolution of Scorpion Potassium Channel Toxins*
    • 45
    • PDF

    References

    SHOWING 1-10 OF 39 REFERENCES
    Solution structure of BmKTX, a K+ blocker toxin from the Chinese scorpion Buthus Martensi
    • 31
    Crystal structure of an acidic neurotoxin from scorpion Buthus martensii Karsch at 1.85 A resolution.
    • 81
    Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels.
    • 30
    Purification, characterization and structural study of the neuro-peptides from scorpion Buthus martensi Karsch
    • 18
    • PDF
    Solution structure of P01, a natural scorpion peptide structurally analogous to scorpion toxins specific for apamin‐sensitive potassium channel
    • 34
    Solution structure of P05-NH2, a scorpion toxin analog with high affinity for the apamin-sensitive potassium channel.
    • 48
    Characterization of four toxins from Buthus martensi scorpion venom, which act on apamin-sensitive Ca2+-activated K+ channels.
    • 78
    NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels.
    • 132
    • PDF
    Two neurotoxins (BmK I and BmK II) from the venom of the scorpion Buthus martensi Karsch: purification, amino acid sequences and assessment of specific activity.
    • Y. Ji, P. Mansuelle, +4 authors H. Rochat
    • Biology, Medicine
    • Toxicon : official journal of the International Society on Toxinology
    • 1996
    • 102
    Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels.
    • 257
    • PDF