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Science 12 October 1990:
Vol. 250. no. 4978, pp. 276 - 279
DOI: 10.1126/science.2218530
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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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Inactivation of Voltage-Gated Cardiac K+ Channels.
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Molecular Determinants of Stereoselective Bupivacaine Block of hKv1.5 Channels.
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Alternative Splicing in the Pore-Forming Region of shaker Potassium Channels.
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Silver as a probe of pore-forming residues in a potassium channel.
Q Lu and C Miller (1995)
Science 268, 304-307
   Abstract »    PDF »
Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor.
P Hidalgo and R MacKinnon (1995)
Science 268, 307-310
   Abstract »    PDF »
Specification of pore properties by the carboxyl terminus of inwardly rectifying K+ channels.
M Taglialatela, B. Wible, R Caporaso, and A. Brown (1994)
Science 264, 844-847
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)