Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate.
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.
Naur
Peter
P
Biostructural Research, Department of Medicinal Chemistry, Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen, Denmark.
Vestergaard
Bente
B
Skov
Lars K
LK
Egebjerg
Jan
J
Gajhede
Michael
M
Kastrup
Jette Sandholm
JS
D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D019281:Dimerization; D005971:Glutamates / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D018091:Receptors, AMPA / Q000737:chemistry / Q000378:metabolism; D018092:Kainic Acid Receptors / Q000737:chemistry* / Q000378:metabolism*; D016415:Sequence Alignment
D005971:Glutamates; D008024:Ligands; D018091:Receptors, AMPA; D018092:Kainic Acid Receptors; C104722:glutamate receptor ionotropic, AMPA 2