1FTM

CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH AMPA AT 1.7 RESOLUTION

Summary for 1FTM

• Entry DOI: 10.2210/pdb1ftm/pdb
• Related: 1FTJ 1FTK 1FTL 1FTO 1FW0 1GR2
• Descriptor: GLUTAMATE RECEPTOR SUBUNIT 2, ZINC ION, (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID, ... (4 entities in total)
• Functional Keywords: ampa receptor, glur2, s1s2, ligand-binding core, agonist, membrane protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P19491
• Total number of polymer chains: 3
• Total formula weight: 88550.59

Authors

Gouaux, E.,Armstrong, N. (deposition date: 2000-09-12, release date: 2000-11-01, Last modification date: 2024-10-30)

Primary citation

Armstrong, N.,Gouaux, E.
Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core.
Neuron, 28:165-181, 2000

PubMed Abstract: Crystal structures of the GluR2 ligand binding core (S1S2) have been determined in the apo state and in the presence of the antagonist DNQX, the partial agonist kainate, and the full agonists AMPA and glutamate. The domains of the S1S2 ligand binding core are expanded in the apo state and contract upon ligand binding with the extent of domain separation decreasing in the order of apo > DNQX > kainate > glutamate approximately equal to AMPA. These results suggest that agonist-induced domain closure gates the transmembrane channel and the extent of receptor activation depends upon the degree of domain closure. AMPA and glutamate also promote a 180 degrees flip of a trans peptide bond in the ligand binding site. The crystal packing of the ligand binding cores suggests modes for subunit-subunit contact in the intact receptor and mechanisms by which allosteric effectors modulate receptor activity.

PubMed: 11086992
DOI: 10.1016/S0896-6273(00)00094-5

Experimental method

X-RAY DIFFRACTION (1.7 Å)