Crystal structure of the kainate receptor GluR5 ligand‐binding core in complex with ( S )‐glutamate
2005; Wiley; Volume: 579; Issue: 5 Linguagem: Inglês
10.1016/j.febslet.2005.01.012
ISSN1873-3468
AutoresPeter Naur, Bente Vestergaard, Lars K. Skov, Jan Egebjerg, Michael Gajhede, J.S. Kastrup,
Tópico(s)Neuropeptides and Animal Physiology
ResumoThe 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.
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