Molecular determinants of gating at the potassium-channel selectivity filter

Julio F. Cordero-Morales, Luis G. Cuello, Yanxiang Zhao, Vishwanath Jogini, D. Marien Cortes, Benoît Roux, Eduardo Perozo

Research output: Journal article publicationJournal articleAcademic researchpeer-review

374 Citations (Scopus)


We show that in the potassium channel KcsA, proton-dependent activation is followed by an inactivation process similar to C-type inactivation, and this process is suppressed by an E71A mutation in the pore helix. EPR spectroscopy demonstrates that the inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at the selectivity filter. Two E71A crystal structures obtained at 2.5 Å reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of the range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation.
Original languageEnglish
Pages (from-to)311-318
Number of pages8
JournalNature Structural and Molecular Biology
Issue number4
Publication statusPublished - 1 Apr 2006
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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