Rapid intracellular TEA block of the KcsA potassium channel

被引:49
作者
Kutluay, E
Roux, B
Heginbotham, L
机构
[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
[2] Cornell Univ, Weill Sch Med Sci, Dept Biochem, New York, NY 10021 USA
[3] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
关键词
D O I
10.1529/biophysj.104.052043
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Intracellular tetraethylammonium (TEA) inhibition was studied at the single-channel level in the KcsA potassium channel reconstituted in planar lipid bilayers. TEA acts as a fast blocker (resulting in decreased current amplitude) with an affinity in the 75 mM range even at high bandwidth. Studies over a wide voltage range reveal that TEA block has a complex voltage-dependence that also depends on the ionic conditions. These observations are examined in the context of permeation models to extend our understanding of the coupling between permeant ions and TEA blockade.
引用
收藏
页码:1018 / 1029
页数:12
相关论文
共 43 条
[41]   Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors [J].
Zhou, M ;
Morais-Cabral, JH ;
Mann, S ;
MacKinnon, R .
NATURE, 2001, 411 (6838) :657-661
[42]   Ion binding affinity in the cavity of the KcsA potassium channel [J].
Zhou, Y ;
MacKinnon, R .
BIOCHEMISTRY, 2004, 43 (17) :4978-4982
[43]   Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution [J].
Zhou, YF ;
Morais-Cabral, JH ;
Kaufman, A ;
MacKinnon, R .
NATURE, 2001, 414 (6859) :43-48