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Title
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Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate.
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Authors
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P.Naur,
B.Vestergaard,
L.K.Skov,
J.Egebjerg,
M.Gajhede,
J.S.Kastrup.
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Ref.
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FEBS Lett, 2005,
579,
1154-1160.
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PubMed id
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Abstract
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The X-ray structure of the ligand-binding core of the kainate receptor GluR5
(GluR5-S1S2) in complex with (S)-glutamate was determined to 1.95 A 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 degrees) 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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