Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.

ABSTRACT: Glutamate receptor ion channels are membrane proteins that mediate excitatory synaptic transmission in the central nervous system of vertebrates. Insight into molecular mechanisms underlying glutamate receptor gating is limited by lack of structural information for receptors trapped in different conformational states. Here, we report the use of single-particle cryoelectron tomography to determine the structures, at ∼21 Å resolution, of full-length GluK2 kainate receptors trapped in antagonist-bound resting and agonist-bound desensitized states. The resting state, stabilized by the competitive antagonist LY466195, closely resembles the crystal structure of the AMPA receptor GluA2, with well-resolved proximal and distal subunits exhibiting cross-over between the twofold symmetric amino termi

SUBMITTER: Schauder DM 

PROVIDER: S-EPMC3625259 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature