Subtype-dependent N-methyl-D-aspartate receptor amino-terminal domain conformations and modulation by spermine.

ABSTRACT: The N-methyl-d-aspartate (NMDA) subtype of the ionotropic glutamate receptors is the primary mediator of calcium-permeable excitatory neurotransmission in the central nervous system. Subunit composition and binding of allosteric modulators to the amino-terminal domain determine the open probability of the channel. By using luminescence resonance energy transfer with functional receptors expressed in CHO cells, we show that the cleft of the amino-terminal domain of the GluN2B subunit, which has a lower channel open probability, is on average more closed than the GluN2A subunit, which has a higher open probability. Furthermore, the GluN1 amino-terminal domain adopts a more open conformation when coassembled with GluN2A than with GluN2B. Binding of spermine, an allosteric potentiator, opens t

SUBMITTER: Sirrieh RE 

PROVIDER: S-EPMC4432297 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature