1TXF

CRYSTAL STRUCTURE OF THE GLUR5 LIGAND BINDING CORE IN COMPLEX WITH GLUTAMATE AT 2.1 ANGSTROM RESOLUTION

Summary for 1TXF

• Entry DOI: 10.2210/pdb1txf/pdb
• Related: 1FTJ 1II5 1S50 1S7Y 1S9T 1SD3 1TT1
• Descriptor: Glutamate receptor, ionotropic kainate 1, GLUTAMIC ACID (3 entities in total)
• Functional Keywords: membrane protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P22756
• Total number of polymer chains: 1
• Total formula weight: 29400.69

Authors

Mayer, M.L. (deposition date: 2004-07-04, release date: 2005-02-08, Last modification date: 2023-08-23)

Primary citation

Mayer, M.L.
Crystal structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity
Neuron, 45:539-552, 2005

PubMed Abstract: Little is known about the molecular mechanisms underlying differences in the ligand binding properties of AMPA, kainate, and NMDA subtype glutamate receptors. Crystal structures of the GluR5 and GluR6 kainate receptor ligand binding cores in complexes with glutamate, 2S,4R-4-methylglutamate, kainate, and quisqualate have now been solved. The structures reveal that the ligand binding cavities are 40% (GluR5) and 16% (GluR6) larger than for GluR2. The binding of AMPA- and GluR5-selective agonists to GluR6 is prevented by steric occlusion, which also interferes with the high-affinity binding of 2S,4R-4-methylglutamate to AMPA receptors. Strikingly, the extent of domain closure produced by the GluR6 partial agonist kainate is only 3 degrees less than for glutamate and 11 degrees greater than for the GluR2 kainate complex. This, together with extensive interdomain contacts between domains 1 and 2 of GluR5 and GluR6, absent from AMPA receptors, likely contributes to the high stability of GluR5 and GluR6 kainate complexes.

PubMed: 15721240
DOI: 10.1016/j.neuron.2005.01.031

Experimental method

X-RAY DIFFRACTION (2.1 Å)