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Allosteric coupling of the inner activation gate to the outer pore of a potassium channel.

ABSTRACT: In potassium channels, functional coupling of the inner and outer pore gates may result from energetic interactions between residues and conformational rearrangements that occur along a structural path between them. Here, we show that conservative mutations of a residue near the inner activation gate of the Shaker potassium channel (I470) modify the rate of C-type inactivation at the outer pore, pointing to this residue as part of a pathway that couples inner gate opening to changes in outer pore structure and reduction of ion flow. Because they remain equally sensitive to rises in extracellular potassium, altered inactivation rates of the mutant channels are not secondary to modified binding of potassium to the outer pore. Conservative mutations of I470 also influence the interaction of the Shaker N-terminus with the inner gate, which separately affects the outer pore.

SUBMITTER: Peters CJ

PROVIDER: S-EPMC3806241 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Allosteric coupling of the inner activation gate to the outer pore of a potassium channel.

Peters Christian J CJ Fedida David D Accili Eric A EA

Scientific reports 20131023

In potassium channels, functional coupling of the inner and outer pore gates may result from energetic interactions between residues and conformational rearrangements that occur along a structural path between them. Here, we show that conservative mutations of a residue near the inner activation gate of the Shaker potassium channel (I470) modify the rate of C-type inactivation at the outer pore, pointing to this residue as part of a pathway that couples inner gate opening to changes in outer por ...[more]

PMID: 24149575

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