1yae
From Proteopedia
(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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| - | [[Image:1yae.gif|left|200px]]<br /><applet load="1yae" size=" | + | [[Image:1yae.gif|left|200px]]<br /><applet load="1yae" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yae, resolution 3.11Å" /> | caption="1yae, resolution 3.11Å" /> | ||
'''Structure of the Kainate Receptor Subunit GluR6 Agonist Binding Domain Complexed with Domoic Acid'''<br /> | '''Structure of the Kainate Receptor Subunit GluR6 Agonist Binding Domain Complexed with Domoic Acid'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the crystal structure of the glycosylated ligand-binding (S1S2) | + | 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== | ==About this Structure== | ||
| - | 1YAE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAG and DOQ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YAE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=DOQ:'>DOQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YAE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Choe, S.]] | [[Category: Choe, S.]] | ||
[[Category: Green, T.]] | [[Category: Green, T.]] | ||
| - | [[Category: Heinemann, S | + | [[Category: Heinemann, S F.]] |
| - | [[Category: Nanao, M | + | [[Category: Nanao, M H.]] |
[[Category: Stern-Bach, Y.]] | [[Category: Stern-Bach, Y.]] | ||
[[Category: DOQ]] | [[Category: DOQ]] | ||
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[[Category: kainate receptor]] | [[Category: kainate receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:17 2008'' |
Revision as of 14:03, 21 February 2008
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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 and 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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