A Strongly Interacting Pair of Residues on the Contact Surface of Charybdotoxin and a Shaker K+ Channel

  title={A Strongly Interacting Pair of Residues on the Contact Surface of Charybdotoxin and a Shaker K+ Channel},
  author={D. Naranjo and C. Miller},
  • D. Naranjo, C. Miller
  • Published 1996
  • Chemistry, Medicine
  • Neuron
  • Charybdotoxin, a peptide neurotoxin of known molecular structure, blocks Shaker K+ channels by binding to a receptor at the outer opening of the ion conduction pathway. Analysis of variants of CTX at position 29 and of Shaker at position 449 shows that these two residues interact closely in the channel-toxin complex. The CTX mutation M29I leads to a slight strengthening of block when tested on Shaker-449T; the same CTX mutation weakens block 1700-fold when tested on Shaker-449F. The known… CONTINUE READING
    126 Citations

    Figures and Topics from this paper

    Electrostatic interaction between charybdotoxin and a tetrameric mutant of Shaker K(+) channels.
    • 14
    Proton Probing of the Charybdotoxin Binding Site of Shaker K+ Channels
    • 17
    • PDF
    A Model of Scorpion Toxin Binding to Voltage-gated K+ Channels
    • 34
    • Highly Influenced
    The Signature Sequence of Voltage-gated Potassium Channels Projects into the External Vestibule*
    • 119
    • PDF


    The charybdotoxin receptor of a Shaker K+ channel: Peptide and channel residues mediating molecular recognition
    • 261
    Intimations of K+ channel structure from a complete functional map of the molecular surface of charybdotoxin.
    • 165
    Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor.
    • 319
    Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor.
    • 406
    • Highly Influential
    Solution structure of the potassium channel inhibitor agitoxin 2: Caliper for probing channel geometry
    • 104
    • PDF
    The aromatic binding site for tetraethylammonium ion on potassium channels
    • 402
    • Highly Influential