Crystal structure of the kainate receptor GluR5 ligand‐binding core in complex with (S)‐glutamate
Open Access
- 19 January 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (5) , 1154-1160
- https://doi.org/10.1016/j.febslet.2005.01.012
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 1.95 Å 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.Keywords
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