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Science 12 October 1990:
Vol. 250. no. 4978, pp. 276 - 279
DOI: 10.1126/science.2218530

Articles

Science, Vol 250, Issue 4978, 276-279
Copyright © 1990 by American Association for the Advancement of Science


articles

Mutations affecting TEA blockade and ion permeation in voltage-activated K+ channels

R MacKinnon and G Yellen

Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, MA 02115.

Voltage-dependent ion channels are responsible for electrical signaling in neurons and other cells. The main classes of voltage-dependent channels (sodium-, calcium-, and potassium-selective channels) have closely related molecular structures. For one member of this superfamily, the transiently voltage-activated Shaker H4 potassium channel, specific amino acid residues have now been identified that affect channel blockade by the small ion tetraethylammonium, as well as the conduction of ions through the pore. Furthermore, variation at one of these amino acid positions among naturally occurring potassium channels may account for most of their differences in sensitivity to tetraethylammonium.


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Silver as a probe of pore-forming residues in a potassium channel.
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P Hidalgo and R MacKinnon (1995)
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Specification of pore properties by the carboxyl terminus of inwardly rectifying K+ channels.
M Taglialatela, B. Wible, R Caporaso, and A. Brown (1994)
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A mechanism for ion selectivity in potassium channels: computational studies of cation-pi interactions.
R. Kumpf and D. Dougherty (1993)
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mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels.
A Butler, S Tsunoda, D. McCobb, A Wei, and L Salkoff (1993)
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Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA.
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A functional connection between the pores of distantly related ion channels as revealed by mutant K+ channels.
L Heginbotham, T Abramson, and R MacKinnon (1992)
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Ion channel structure and function.
C Miller (1992)
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Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel.
M Li, Y. Jan, and L. Jan (1992)
Science 257, 1225-1230
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A Mutant of TTX-Resistant Cardiac Sodium Channels with TTX-Sensitive Properties.
J. Satin, J. W. Kyle, M. Chen, P. Bell, L. L. Cribbs, H. A. Fozzard, and R. B. Rogart (1992)
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Cloning and expression in yeast of a plant potassium ion transport system.
H Sentenac, N Bonneaud, M Minet, F Lacroute, J. Salmon, F Gaymard, and C Grignon (1992)
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A component of calcium-activated potassium channels encoded by the Drosophila slo locus.
N. Atkinson, G. Robertson, and B Ganetzky (1991)
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A distinct potassium channel polypeptide encoded by the Drosophila eag locus.
J Warmke, R Drysdale, and B Ganetzky (1991)
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Mutations affecting internal TEA blockade identify the probable pore-forming region of a K+ channel.
G Yellen, M. Jurman, T Abramson, and R MacKinnon (1991)
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Exchange of conduction pathways between two related K+ channels.
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Flexibility of the Kir6.2 inward rectifier K+ channel pore.
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