K+ pore structure revealed by reporter cysteines at inner and outer surfaces

Juan M. Pascual, Char Chang Shieh, Glenn E. Kirsch, Arthur M. Brown

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Abstract

The structure of the carboxyl half of the pore-forming region of Kv2.1 was studied by replacing each of 15 consecutive residues between positions 383 and 369 with a reporter cysteine residue. Extracellular application of charged, membrane-impermeant methanethiosulfonates irreversibly modified currents at four cysteine-substituted positions, K382, Y380,1379, and D378. Intracellular exposure to methanethiosulfonate ethyltrimethylammonium revealed another set of reactive mutants (V374, T373, T372, and T370). Our results indicate that positions 378 and 374 are exposed at outer and inner mouths of the channel, respectively, and immersed in the aqueous phase. In contrast to present topological models, the 383-369 region appears to span the pore mainly as a nonperiodic structure.

Original languageEnglish (US)
Pages (from-to)1055-1063
Number of pages9
JournalNeuron
Volume14
Issue number5
DOIs
StatePublished - May 1995

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ASJC Scopus subject areas

  • Neuroscience(all)

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