Exchange of Conduction Pathways Between Two Related K + Channels
Autor: | Rolf H. Joho, Arthur M. Brown, Mauruzio Taglialatela, Glenn E. Kirsch, J. A. Drewe, H. A. Hartmann |
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Rok vydání: | 1991 |
Předmět: |
BK channel
Potassium Channels Xenopus Molecular Sequence Data Restriction Mapping KcsA potassium channel Mineralogy Polymerase Chain Reaction Membrane Potentials SK channel Sequence Homology Nucleic Acid Animals Amino Acid Sequence Cloning Molecular Multidisciplinary Base Sequence biology Voltage-gated ion channel Chimera Chemistry Inward-rectifier potassium ion channel Brain Tetraethylammonium Voltage-gated potassium channel Tetraethylammonium Compounds Tandem pore domain potassium channel Calcium-activated potassium channel Rats Oocytes biology.protein Biophysics Female Oligonucleotide Probes Ion Channel Gating |
Zdroj: | Science. 251:942-944 |
ISSN: | 1095-9203 0036-8075 |
DOI: | 10.1126/science.2000495 |
Popis: | 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. |
Databáze: | OpenAIRE |
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