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1FTO

CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE AT 2.0 A RESOLUTION

Summary for 1FTO
Entry DOI10.2210/pdb1fto/pdb
Related1FTJ 1FTK 1FTL 1FTM 1FW0 1GR2
DescriptorGLUTAMATE RECEPTOR SUBUNIT 2 (2 entities in total)
Functional Keywordsionotropic glutamate receptor, unligandeded, apo, ligand binding domain, membrane protein
Biological sourceRattus norvegicus (Norway rat)
More
Cellular locationCell membrane; Multi-pass membrane protein: P19491
Total number of polymer chains2
Total formula weight58443.36
Authors
Armstrong, N.,Gouaux, E. (deposition date: 2000-09-12, release date: 2000-11-01, Last modification date: 2024-11-06)
Primary citationArmstrong, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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