Functional Consequences of a Decreased Potassium Affinity in a Potassium Channel Pore
نویسندگان
چکیده
منابع مشابه
Functional Consequences of a Decreased Potassium Affinity in a Potassium Channel Pore
Ions bound near the external mouth of the potassium channel pore impede the C-type inactivation conformational change (Lopez-Barneo, J., T. Hoshi, S. Heinemann, and R. Aldrich. 1993. Receptors Channels. 1:61- 71; Baukrowitz, T., and G. Yellen. 1995. Neuron. 15:951-960). In this study, we present evidence that the occupancy of the C-type inactivation modulatory site by permeant ions is not solel...
متن کاملFunctional Consequences of a Decreased Potassium Affinity in a Potassium Channel Pore Ion Interactions and C-Type Inactivation
Ions bound near the external mouth of the potassium channel pore impede the C-type inactivation conformational change (Lopez-Barneo, J., T. Hoshi, S. Heinemann, and R. Aldrich. 1993. Receptors Channels. 1:61– 71; Baukrowitz, T., and G. Yellen. 1995. Neuron. 15:951–960). In this study, we present evidence that the occupancy of the C-type inactivation modulatory site by permeant ions is not solel...
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MinK has neither the P region nor signature sequence that characterizes pore-forming subunits of all known K+ channels. A specific minK region has now been identified that affects external blockade by 2 common probes of K+ channel pores. When mutated to cysteine, residues in this region render minK susceptible to covalent blockade by methanethiosulfonate ethylsulfonate and alter reversible inhi...
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In voltage-dependent K+ channels, each of the four identical subunits contributes one pore loop to the central ion selectivity unit at the interface between the subunits. The pore loop is also the target for scorpion venom peptide inhibitors. These inhibitors bind at the pore entryway between the four subunits and can assume any one of four orientations. The orientations become distinguishable ...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1999
ISSN: 0022-1295,1540-7748
DOI: 10.1085/jgp.113.2.347