3H6G

Crystal structure of the GluR6 amino terminal domain dimer assembly

Summary for 3H6G

• Entry DOI: 10.2210/pdb3h6g/pdb
• Related: 3H5V 3H5W 3H6H 3c32
• Descriptor: Glutamate receptor, ionotropic kainate 2, 2-acetamido-2-deoxy-beta-D-glucopyranose, L(+)-TARTARIC ACID, ... (5 entities in total)
• Functional Keywords: membrane protein glycoprotein, cell junction, cell membrane, glycoprotein, ion transport, ionic channel, isopeptide bond, membrane, postsynaptic cell membrane, receptor, rna editing, synapse, transmembrane, transport, membrane protein
• Biological source: Rattus norvegicus (rat)
• Total number of polymer chains: 2
• Total formula weight: 91650.24

Authors

Kumar, J.,Mayer, M.L. (deposition date: 2009-04-23, release date: 2009-05-26, Last modification date: 2024-11-06)

Primary citation

Kumar, J.,Schuck, P.,Jin, R.,Mayer, M.L.
The N-terminal domain of GluR6-subtype glutamate receptor ion channels.
Nat.Struct.Mol.Biol., 16:631-638, 2009

PubMed Abstract: The amino-terminal domain (ATD) of glutamate receptor ion channels, which controls their selective assembly into AMPA, kainate and NMDA receptor subtypes, is also the site of action of NMDA receptor allosteric modulators. Here we report the crystal structure of the ATD from the kainate receptor GluR6. The ATD forms dimers in solution at micromolar protein concentrations and crystallizes as a dimer. Unexpectedly, each subunit adopts an intermediate extent of domain closure compared to the apo and ligand-bound complexes of LIVBP and G protein-coupled glutamate receptors (mGluRs), and the dimer assembly has a markedly different conformation from that found in mGluRs. This conformation is stabilized by contacts between large hydrophobic patches in the R2 domain that are absent in NMDA receptors, suggesting that the ATDs of individual glutamate receptor ion channels have evolved into functionally distinct families.

PubMed: 19465914
DOI: 10.1038/nsmb.1613

Experimental method

X-RAY DIFFRACTION (2.697 Å)