Article abstract


Nature Structural & Molecular Biology 14, 1062 - 1069 (2007)
Published online: 7 October 2007 | doi:10.1038/nsmb1309

Molecular driving forces determining potassium channel slow inactivation

Julio F Cordero-Morales1,2,3, Vishwanath Jogini2,3, Anthony Lewis2, Valeria Vásquez1,2, D Marien Cortes2, Benoît Roux2 & Eduardo Perozo2


K+ channels undergo a time-dependent slow inactivation process that plays a key role in modulating cellular excitability. Here we show that in the prokaryotic proton-gated K+ channel KcsA, the number and strength of hydrogen bonds between residues in the selectivity filter and its adjacent pore helix determine the rate and extent of C-type inactivation. Upon channel activation, the interaction between residues at positions Glu71 and Asp80 promotes filter constriction parallel to the permeation pathway, which affects K+-binding sites and presumably abrogates ion conduction. Coupling between these two positions results in a quantitative correlation between their interaction strength and the stability of the inactivated state. Engineering of these interactions in the eukaryotic voltage-dependent K+ channel Kv1.2 suggests that a similar mechanistic principle applies to other K+ channels. These observations provide a plausible physical framework for understanding C-type inactivation in K+ channels.

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  1. Department of Molecular Physiology and Biological Physics, University of Virginia, 1300 JPA, Charlottesville, Virginia 22908, USA.
  2. Institute for Molecular Pediatric Sciences, Institute for Biophysical Dynamics and Department of Biochemistry and Molecular Biology, The University of Chicago, 929 E. 57th Street, Chicago, Illinois 60637, USA.
  3. These authors contributed equally to this work.

Correspondence to: Eduardo Perozo2 e-mail: eperozo@uchicago.edu



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