Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10873660 | FEBS Letters | 2005 | 7 Pages |
Abstract
The X-ray structure of the ligand-binding core of the kainate receptor GluR5 (GluR5-S1S2) in complex with (S)-glutamate was determined to 1.95Â Ã
resolution. The overall GluR5-S1S2 structure comprises two domains and is similar to the related AMPA receptor GluR2-S1S2J. (S)-glutamate binds as in GluR2-S1S2J. Distinct features are observed for Ser741, which stabilizes a highly coordinated network of water molecules and forms an interdomain bridge. The GluR5 complex exhibits a high degree of domain closure (26°) relative to apo GluR2-S1S2J. In addition, GluR5-S1S2 forms a novel dimer interface with a different arrangement of the two protomers compared to GluR2-S1S2J.
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Authors
Peter Naur, Bente Vestergaard, Lars K. Skov, Jan Egebjerg, Michael Gajhede, Jette Sandholm Kastrup,