2uxa

File:2uxa.gif

spinqualitylabelsall models 2uxa, resolution 2.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE GLUR2-FLIP LIGAND BINDING DOMAIN, R/G UNEDITED.

OverviewOverview

The subunit composition determines AMPA receptor (AMPA-R) function and, trafficking. Mechanisms underlying channel assembly are thus central to, the efficacy and plasticity of glutamatergic synapses. We previously, showed that RNA editing at the Q/R site of the GluR2 subunit contributes, to the assembly of AMPA-R heteromers by attenuating formation of GluR2, homotetramers. Here we report that this function of the Q/R site depends, on subunit contacts between adjacent ligand binding domains (LBDs)., Changes of LBD interface contacts alter GluR2 assembly properties, forward, traffic, and expression at synapses. Interestingly, developmentally, regulated RNA editing within the LBD (at the R/G site) produces analogous, effects. Our data reveal that editing to glycine reduces the self-assembly, competence of this critical subunit and slows GluR2 maturation in the, endoplasmic reticulum (ER). Therefore, RNA editing sites, located at, strategic subunit interfaces, shape AMPA-R assembly and trafficking in a, developmentally regulated manner.

About this StructureAbout this Structure

2UXA is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Known structural/functional Sites: , , , , , , and . Full crystallographic information is available from OCA.

ReferenceReference

Developmentally regulated, combinatorial RNA processing modulates AMPA receptor biogenesis., Greger IH, Akamine P, Khatri L, Ziff EB, Neuron. 2006 Jul 6;51(1):85-97. PMID:16815334

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