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Structural rearrangements underlying ligand-gating in Kir channels

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  • Shizhen Wang

    (Washington University School of Medicine
    Saint Louis University)

  • Sun-Joo Lee

    (Washington University School of Medicine)

  • Sarah Heyman

    (Washington University School of Medicine)

  • Decha Enkvetchakul

    (Saint Louis University)

  • Colin G. Nichols

    (Washington University School of Medicine)

Abstract

Inward rectifier potassium (Kir) channels are physiologically regulated by a wide range of ligands that all act on a common gate, although structural details of gating are unclear. Here we show, using small molecule fluorescent probes attached to introduced cysteines, the molecular motions associated with gating of KirBac1.1 channels. The accessibility of the probes indicates a major barrier to fluorophore entry to the inner cavity. Changes in fluorescence resonance energy transfer between fluorophores, attached to KirBac1.1 tetramers, show that phosphatidylinositol-4,5-bisphosphate-induced closure involves tilting and rotational motions of secondary structural elements of the cytoplasmic domain that couple ligand binding to a narrowing of the cytoplasmic vestibule. The observed ligand-dependent conformational changes in KirBac1.1 provide a general model for ligand-induced Kir channel gating at the molecular level.

Suggested Citation

  • Shizhen Wang & Sun-Joo Lee & Sarah Heyman & Decha Enkvetchakul & Colin G. Nichols, 2012. "Structural rearrangements underlying ligand-gating in Kir channels," Nature Communications, Nature, vol. 3(1), pages 1-8, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1625
    DOI: 10.1038/ncomms1625
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