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Published online April 16, 2007
doi:10.1085/jgp.200709758
The Journal of General Physiology, Vol. 129, No. 5, 403-418
The Rockefeller University Press, 0022-1295 $30.00
© 2007 Panyi et al.
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ARTICLE

 Probing the Cavity of the Slow Inactivated Conformation of Shaker Potassium Channels



Gyorgy Panyi and Carol Deutsch

Department of Biophysics and Cell Biology, University of Debrecen, Debrecen, Hungary
Department of Physiology, University of Pennsylvania, Philadelphia, PA 19104

Correspondence to Carol Deutsch: cjd{at}mail.med.upenn.edu

Slow inactivation involves a local rearrangement of the outer mouth of voltage-gated potassium channels, but nothing is known regarding rearrangements in the cavity between the activation gate and the selectivity filter. We now report that the cavity undergoes a conformational change in the slow-inactivated state. This change is manifest as altered accessibility of residues facing the aqueous cavity and as a marked decrease in the affinity of tetraethylammonium for its internal binding site. These findings have implications for global alterations of the channel during slow inactivation and putative coupling between activation and slow-inactivation gates.

Abbreviations used in this paper: DMPS, 2,3-dimercapto-1-propane sulfonic acid; MTSEA, ethylammonium methanethiosulfonate; MTSET, ethyltrimethylammonium methanethiosulfonate; QA, quaternary ammonium.


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