First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
|1ftl, resolution 1.80Å ()|
|Related:||1gr2, 1ftj, 1ftk, 1ftm, 1fto, 1fw0|
CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH THE ANTAGONIST DNQX AT 1.8 A RESOLUTION
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Armstrong N, Gouaux E. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron. 2000 Oct;28(1):165-81. PMID:11086992
- Madden DR. The structure and function of glutamate receptor ion channels. Nat Rev Neurosci. 2002 Feb;3(2):91-101. PMID:11836517 doi:10.1038/nrn725