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Gambierol and n-alkanols inhibit Shaker Kv channel via distinct binding sites outside the K+ pore
Martínez-Morales, E.; Kopljar, I.; Rainier, J.D.; Tytgat, J.; Snyders, D.J.; Labro, A.J. (2016). Gambierol and n-alkanols inhibit Shaker Kv channel via distinct binding sites outside the K+ pore. Toxicon 120: 57-60. https://dx.doi.org/10.1016/j.toxicon.2016.07.017
In: Toxicon. Elsevier: Oxford. ISSN 0041-0101; e-ISSN 1879-3150
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoord
    Marien/Kust
Author keywords
    Potassium channel; Gating modifier; Lipophilic marine toxin; 1-Alcohol;Electrophysiology
Auteurs  Top 
  • Martínez-Morales, E.
  • Kopljar, I.
  • Rainier, J.D.
  • Tytgat, J., meer
  • Snyders, D.J.
  • Labro, A.J.
Abstract
    The marine polycyclic-ether toxin gambierol and 1-butanol (n-alkanol) inhibit Shaker-type Kv channels by interfering with the gating machinery. Competition experiments indicated that both compounds do not share an overlapping binding site but gambierol is able to affect 1-butanol affinity for Shaker through an allosteric effect. Furthermore, the Shaker-P475A mutant, which inverses 1-butanol effect, is inhibited by gambierol with nM affinity. Thus, gambierol and 1-butanol inhibit Shaker-type Kv channels via distinct parts of the gating machinery.
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