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K+ occupancy of the N-methylaspartate- D-aspartate receptor channel probed by Mg2+ block


, : K+ occupancy of the N-methylaspartate- D-aspartate receptor channel probed by Mg2+ block. The Journal of General Physiology 117(3): 7-97

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 [similar]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 [similar]1,400-fold apparent decrease in the affinity of the channel for extracellular Mg2+ and [similar]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. Reprinted by permission of the publisher.

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