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 1.95Å 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-...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	FEBS letters 2005-02, Vol.579 (5), p.1154-1160
Hauptverfasser:	Naur, Peter, Vestergaard, Bente, Skov, Lars K., Egebjerg, Jan, Gajhede, Michael, Kastrup, Jette Sandholm
Format:	Artikel
Sprache:	eng
Schlagworte:	2-amino-3-(3-hydroxy-5-methyl-4-isoxazolyl)propionate 2-amino-3-(3-hydroxy-7,8-dihydro-6H-cyclohepta[d]-4-isoxazolyl)propionate 2-amino-3-(5-tert-butyl-3-hydroxy-4-isoxazolyl)propionate 4-AHCP Amino Acid Sequence AMPA ATPA Binding Sites Crystal structure Crystallography, X-Ray Dimerization E. coli EDTA Escherichia coli ethylenediaminetetraacetate GluR2-S1S2J GluR5 ligand-binding core GluR5-S1S2 Glutamates - metabolism HEPES iGluR Ionotropic glutamate receptor IPTG isopropyl-β-d-thiogalactopyranoside Kainate receptor ligand-binding core construct of GluR2 ligand-binding core construct of GluR5 ligand-binding core construct of NR1 Ligands M1–M3 Models, Molecular Molecular Sequence Data N-2-hydroxyethylpiperazine-N′-2-ethanesulfonate N-methyl-d-aspartate NMDA NR1-S1S2 PCR PEG polyethylene glycol polymerase chain reaction Protein Structure, Quaternary r.m.s.d Receptors, AMPA - chemistry Receptors, AMPA - metabolism Receptors, Kainic Acid - chemistry Receptors, Kainic Acid - metabolism root mean square deviation Sequence Alignment three transmembrane spanning regions van der Waals vdW
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	The X-ray structure of the ligand-binding core of the kainate receptor GluR5 (GluR5-S1S2) in complex with (S)-glutamate was determined to 1.95Å 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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2005.01.012