Semiclosed Conformations of the Ligand-Binding Domains of NMDA Receptors during Stationary Gating.

ABSTRACT: NMDA receptors are tetrameric ligand-gated ion channels. In the continuous presence of saturating agonists, NMDA receptors undergo stationary gating, in which the channel stochastically switches between an open state that permits ion conductance and a closed state that prevents permeation. The ligand-binding domains (LBDs) of the four subunits are expected to have closed clefts in the channel-open state. On the other hand, there is little knowledge about the conformational status of the LBDs in the channel-closed state during stationary gating. To probe the latter conformational status, Kussius and Popescu engineered interlobe disulfide cross-links in NMDA receptors and found that the cross-linking produced stationary gating kinetics that differed only subtly from that produced by agonist

SUBMITTER: Dai J 

PROVIDER: S-EPMC5052434 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature