1yae
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(New page: 200px<br /><applet load="1yae" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yae, resolution 3.11Å" /> '''Structure of the Kai...)
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Revision as of 04:31, 21 November 2007
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Structure of the Kainate Receptor Subunit GluR6 Agonist Binding Domain Complexed with Domoic Acid
Overview
We report the crystal structure of the glycosylated ligand-binding (S1S2), domain of the kainate receptor subunit GluR6, in complex with the agonist, domoate. The structure shows the expected overall homology with AMPA and, NMDA receptor subunit structures but reveals an unexpected binding mode, for the side chain of domoate, in which contact is made to the larger lobe, only (lobe I). In common with the AMPA receptor subunit GluR2, the GluR6, S1S2 domain associates as a dimer, with many of the interdimer contacts, being conserved. Subtle differences in these contacts provide a structural, explanation for why GluR2 L483Y and GluR3 L507Y are nondesensitizing, but, GluR6, which has a tyrosine at that site, is not. The structure, incorporates native glycosylation, which has not previously been described, for ionotropic glutamate receptors. The position of the sugars near the, subunit interface rules out their direct involvement in subunit, association but leaves open the possibility of indirect modulation., Finally, we observed several tetrameric assemblies that satisfy, topological constraints with respect to connection to the receptor pore, and which are therefore candidates for the native quaternary structure.
About this Structure
1YAE is a Single protein structure of sequence from Rattus norvegicus with NAG and DOQ as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid., Nanao MH, Green T, Stern-Bach Y, Heinemann SF, Choe S, Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1708-13. Epub 2005 Jan 26. PMID:15677325
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