X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with the antagonist (S)-ATPO at 2.1 A resolution.

(S)-2-AMINO-3-(5-TERT-BUTYL-3-(PHOSPHONOMETHOXY)-4-ISOXAZOLYL)PROPIONIC ACID

Competitive antagonism of AMPA receptors by ligands of different classes: crystal structure of ATPO bound to the GluR2 ligand-binding core, in comparison with DNQX.

Structural basis for AMPA receptor activation and ligand selectivity: Crystal structures of five agonist complexes with the GluR2 ligand binding core.

Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core.

Mechanism of glutamate receptor desensitization.

Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct.

GluR-2, GluR-B, Glutamate receptor ionotropic, AMPA 2

GANKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVY
GKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWT
YMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLK
LNEQGLLDKLKNKWWYDKGECGS

PEG 3350, AMMONIUM SULFATE, SODIUM ACETATE pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 279K

GluR2 S1S2J in complex with the agonist glutamate.

GluR2 S1S2I in complex with the agonist kainate.

GluR2 S1S2J in complex with the agonist kainate.

GluR2 S1S2J in complex with the agonist AMPA.

GluR2 S1S2J in complex with the antagonist DNQX.

Non-desensitizing form of GluR2 S1S2J-L483Y in complex with the agonist AMPA.

GluR2 S1S2J-N775S in complex with Cyclothiazide.

GluR2 S1S2J in complex with the agonist ACPA.

GluR2 S1S2J in complex with the agonist Br-HIBO.

GluR2 S1S2J-Y702F in complex with the agonist Br-HIBO.

GluR2 S1S2J-Y702F in complex with the agonist ACPA.

GluR2 S1S2J in complex with quisqualate.

GluR2 S1S2J in complex with the agonist 2-Me-Tet-AMPA.

GluR2 S1S2J-N754D in complex with the agonist kainate.

Native GluR2 is a membrane protein. The protein crystallized is the extracellular ligand-binding core of GluR2. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker (residues 118-119). Therefore, the sequence matches discontinuously with the reference database (413-527, 653-796). The two first residues (Gly, Ala) are cloning artifacts and were not located in the electron density map.

RESIDUES 1-4 AND 262-263 WERE NOT LOCATED IN THE ELECTRON DENSITY MAP. THE SIDE CHAINS OF THE FOLLOWING RESIDUES ARE NOT FULLY DEFINED: LYS A21, MET A25, LYS A69, ARG A149, ARG A163, LYS A204, LYS B21, MET B25, LYS B45, ASP B67, LYS B69, ASP B139, ARG B149, LYS B151, ARG B172, LYS C21, GLU C24, LYS C151, LYS D21, GLU D24, LYS D50, ARG D149, LYS D151, ARG D172, LYS D183.

Ionotropic glutamate receptor GluR2, ligand-binding core, antagonist complex, MEMBRANE PROTEIN

NKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGK
ADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRS
AEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQ
GLLDKLKNKWWYDKGECGS