K(+) occupancy of the N-methyl-d-aspartate receptor channel probed by Mg(2+) block.

K(+) occupancy of the N-methyl-d-aspartate receptor channel probed by Mg(2+) block.
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Mg(2+)块探测的N-甲基-D-天冬氨酸受体通道的K(+)占用率。

DOI:
10.1085/jgp.117.3.287
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发表时间:
2001-03
期刊:
The Journal of general physiology
影响因子:
--
通讯作者:
Auerbach A
Auerbach A
中科院分区:
其他
文献类型:
--
作者:
Zhu Y;Auerbach A

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采用细胞外Mg ~(2+)阻断的单通道动力学方法,研究了大鼠重组NR 1/NR 2B NMDA受体通道渗透途径中的K ~+结合位点。K+结合到三个位点:两个是外部的,一个是内部的Mg 2+块的网站。从细胞外表面通过电场的内部位点为10.84。该位点对K+的平衡解离常数为304 mM(0 mV),且孔中存在Mg 2+。三个位点中的任何一个被K+占据都有效地阻止了胞外Mg 2+的缔合。内部位点的占据还防止Mg 2+渗透并增加(约7倍)Mg 2+解离回到细胞外溶液的速率常数。在生理细胞内离子条件下,在-60 mV时,通道对细胞外Mg 2+的亲和力明显降低了1,400倍,而外部和内部位点的K+占据的电压依赖性导致Mg 2+阻滞的电压依赖性明显增强了1,400倍。
The single-channel kinetics of extracellular Mg2+ block was used to probe K+ binding sites in the permeation pathway of rat recombinant NR1/NR2B NMDA receptor channels. K+ binds to three sites: two that are external and one that is internal to the site of Mg2+ block. The internal site is ∼0.84 through the electric field from the extracellular surface. The equilibrium dissociation constant for this site for K+ is 304 mM at 0 mV and with Mg2+ in the pore. The occupancy of any one of the three sites by K+ effectively prevents the association of extracellular Mg2+. Occupancy of the internal site also prevents Mg2+ permeation and increases (by approximately sevenfold) the rate constant for Mg2+ dissociation back to the extracellular solution. Under physiological intracellular ionic conditions and at −60 mV, there is ∼1,400-fold apparent decrease in the affinity of the channel for extracellular Mg2+ and ∼2-fold enhancement of the apparent voltage dependence of Mg2+ block caused by the voltage dependence of K+ occupancy of the external and internal sites.
DOI: 10.1126/science.280.5360.69
发表时间: 1998-04-03
期刊: SCIENCE
影响因子: 56.9
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离散的BA2+块作为高导通Ca2+活化的K+通道中离子占用和孔结构的探针。
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