1fw0
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CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH KAINATE AT 2.0 A RESOLUTION
OverviewOverview
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.
About this StructureAbout this Structure
1FW0 is a Single protein structure of sequence from Rattus norvegicus with KAI as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core., Armstrong N, Gouaux E, Neuron. 2000 Oct;28(1):165-81. PMID:11086992
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