Brand  (β version)

PDB ID: 1XHY

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Ligands
Code Name Style Show Link
KAI 3-(carboxymethyl)-4-isopropenylproline PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
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Structure summary

Code : 1XHY   PDBj   RCSB PDB   PDBe
Header : MEMBRANE PROTEIN
Title : X-ray structure of the Y702F mutant of the GluR2 ligand-binding core (S1S2J) in complex with kainate at 1.85 A resolution
Release Data : 2005-03-22
Compound :
mol_id molecule chains synonym
1 Glutamate receptor A GluR-2,AMPA-selective glutamate receptor 2,GluR-B,GluR-K2,Glutamate receptor ionotropic,AMPA 2,GluA2,GluR-2,AMPA-selective glutamate receptor 2,GluR-B,GluR-K2,Glutamate receptor ionotropic,AMPA 2,GluA2
fragment: GluR2 flop ligand-binding core (S1S2J), UNP residues 413-527 and 653-796
mutation: Y702F
Source :
mol_id organism_scientific organism_common expression_system
1 Rattus norvegicus  (taxid:10116) Rat Escherichia coli BL21(DE3)  (taxid:469008)
gene: Gria2, Glur2
expression_system_strain: BL21(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: PET30B
Authors : Frandsen, A., Pickering, D.S., Vestergaard, B., Kasper, C., Nielsen, B.B., Greenwood, J.R., Campiani, G., Gajhede, M., Schousboe, A., Kastrup, J.S.
Keywords : Ionotropic glutamate receptor GluR2, mutant, ligand-binding core, kainate complex, MEMBRANE PROTEIN
Exp. method : X-RAY DIFFRACTION ( 1.85 Å )
Citation :

Tyr702 Is an Important Determinant of Agonist Binding and Domain Closure of the Ligand-Binding Core of GluR2.

Frandsen, A.,Pickering, D.S.,Vestergaard, B.  et al.
(2005)  Mol.Pharmacol.  67 : 703 - 713

PubMed: 15591246
DOI: 10.1124/mol.104.002931

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

Hogner, A.,Kastrup, J.S.,Jin, R.  et al.
(2002)  J.Mol.Biol.  322 : 93

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

Armstrong, N.,Gouaux, E.
(2000)  Neuron  28 : 165

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

Chen, G.Q.,Sun, R.,Jin, R.  et al.
(1998)  Protein Sci.  7 : 2623

Reaction

Chain : A
UniProt : P19491 (GRIA2_RAT)
Reaction : -