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单个天冬氨酸残基在小鼠内向整流钾通道Kir2.1的离子选择性和阻断中的作用。

The role of a single aspartate residue in ionic selectivity and block of a murine inward rectifier K+ channel Kir2.1.

作者信息

Abrams C J, Davies N W, Shelton P A, Stanfield P R

机构信息

Department of Cell Physiology and Pharmacology, University of Leicester, UK.

出版信息

J Physiol. 1996 Jun 15;493 ( Pt 3)(Pt 3):643-9. doi: 10.1113/jphysiol.1996.sp021411.

Abstract
  1. The effects of Rb+ and Cs+ as blocking ions were investigated on wild-type and mutant forms of the inward rectifier K+ channel, IRK1 (Kir2.1). 2. In wild-type channels, Rb+ blockage was voltage dependent, increasing and then falling with increasing hyperpolarization. 3. Rb+ blockage was abolished by replacing Asp172 in the M2 domain of the pore-forming subunit by Asn, but was re-established by a change to Gln, narrowing the pore. Blocking affinity was reduced in D172Q, and was also reduced by replacing Gly168 in M2 by Ala. 4. Cs+ blockage was also abolished in D172N but was re-established in D172Q. 5. There appears to be a balance between charge and pore size in determining whether ions block or permeate. A major part of the selectivity of Kir2.1 is associated with Asp172 in the M2 domain.
摘要
  1. 研究了Rb⁺和Cs⁺作为阻断离子对内向整流钾通道IRK1(Kir2.1)野生型和突变形式的影响。2. 在野生型通道中,Rb⁺阻断是电压依赖性的,随着超极化程度增加先升高后降低。3. 通过将孔形成亚基M2结构域中的Asp172替换为Asn,Rb⁺阻断被消除,但通过改变为Gln又重新建立,使孔变窄。D172Q中的阻断亲和力降低,并且通过将M2中的Gly168替换为Ala也降低了阻断亲和力。4. D172N中Cs⁺阻断也被消除,但在D172Q中重新建立。5. 在决定离子是阻断还是通透方面,电荷和孔径之间似乎存在平衡。Kir2.1选择性的主要部分与M2结构域中的Asp172有关。

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