Crystal structure of the GluK1 ligand-binding domain (S1S2) in complex with the antagonist (S)-2-amino-3-(2-(2-carboxyethyl)-5-chloro-4-nitrophenyl)propionic acid at 2.0 A resolution

(S)-2-amino-3-(2-(2-carboxyethyl)-5-chloro-4-nitrophenyl)propionic acid

Structural and pharmacological characterization of phenylalanine-based AMPA receptor antagonists at kainate receptors

Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate.

The protein crystallized is the extracellular ligand binding domain of GluK1. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker.
Glutamate receptor, ionotropic kainate 1
GluK1 Ligand binding domain (GluK1-S1S2)

17 % PEG4000, 0.1M cacodylic acid, 0.3M lithium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K

Crystal structure of the GluA2 ligand binding domain in complex with an antagonist (S)-2-amino-3-(2-(2-carboxyethyl)-5-chloro-4-nitrophenyl)propionic acid

THE SEQUENCE DATABASE IS P22756-2, ISOFORM GLUR5-2.
THE CRYSTALLIZED PROTEIN CONSISTS OF GLY RESIDUE FOLLOWED
BY RESIDUE 430-544 AND 667-805 FROM THE INTACT RECEPTOR
LINKED BY A GLY-THR DIPEPTIDE. THERE IS A SEQUENCE
CONFLICT AT RESIDUE 34 OF THE CRYSTALLIZED PROTEIN DUE TO
DIFFERENCES IN DATABASE SEQUENCE
(SEE GENBANK ACCESION NO.AAA02874).

ionotropic glutamate receptor, glutamate, membrane, MEMBRANE PROTEIN