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.
复制标题
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:
影响因子:
--
通讯作者:
Auerbach A
中科院分区:
文献类型:
--
作者:
Zhu Y;Auerbach A
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.
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影响因子:
56.9
作者:
Doyle, DA;Cabral, JM;MacKinnon, R
通讯作者:
MacKinnon, R
DOI:
10.1073/pnas.93.24.14170
发表时间:
1996-11-26
影响因子:
11.1
作者:
Sharma, G;Stevens, CF
通讯作者:
Stevens, CF
DOI:
10.1073/pnas.92.11.4882
发表时间:
1995-05-23
影响因子:
11.1
作者:
WOOD, MW;VANDONGEN, HMA;VANDONGEN, AMJ
通讯作者:
VANDONGEN, AMJ
DOI:
10.1085/jgp.117.3.275
发表时间:
2001-03
期刊:
The Journal of general physiology
影响因子:
--
作者:
Zhu Y;Auerbach A
通讯作者:
Auerbach A
影响因子:
3.8
作者:
Neyton, J;Miller, C
通讯作者:
Miller, C