Structural rearrangements underlying ligand-gating in Kir channels

Shizhen Wang, Sun-Joo Lee, Sarah Heyman, Decha Enkvetchakul and Colin G. Nichols ()
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Shizhen Wang: Washington University School of Medicine
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

Nature Communications, 2012, vol. 3, issue 1, 1-8

Abstract: 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.

Date: 2012
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DOI: 10.1038/ncomms1625

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