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Science 22 February 1991:
Vol. 251. no. 4996, pp. 942 - 944
DOI: 10.1126/science.2000495
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Articles

Science, Vol 251, Issue 4996, 942-944
Copyright © 1991 by American Association for the Advancement of Science

articles

Exchange of conduction pathways between two related K+ channels

HA Hartmann, GE Kirsch, JA Drewe, M Taglialatela, RH Joho, and AM Brown

Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030.

The structure of the ion conduction pathway or pore of voltage-gated ion channels is unknown, although the linker between the membrane spanning segments S5 and S6 has been suggested to form part of the pore in potassium channels. To test whether this region controls potassium channel conduction, a 21-amino acid segment of the S5-S6 linker was transplanted from the voltage-activated potassium channel NGK2 to another potassium channel DRK1, which has very different pore properties. In the resulting chimeric channel, the single channel conductance and blockade by external and internal tetraethylammonium (TEA) ion were characteristic of the donor NGK2 channel. Thus, this 21-amino acid segment controls the essential biophysical properties of the pore and may form the conduction pathway of these potassium channels.


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