› 1n0t

X-ray diffraction
2.1Å resolution

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

Released:
DOI: 10.2210/pdb1n0t/pdb
PDB entry 1n0t coloured by chain, front view.
PDB entry 1n0t coloured by chain, side view.
PDB entry 1n0t coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
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.
Hogner A, Greenwood JR, Liljefors T, Lunn ML, Egebjerg J, Larsen IK, Gouaux E, Kastrup JS
J Med Chem 46 214-21 (2003)
PMID: 12519060

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate receptor 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 263 amino acids
Theoretical weight: 29.22 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19491 (Residues: 413-527, 653-796; Coverage: 30%)
Gene names: GluA2, Glur2, Gria2
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

3 bound ligands:
Ligand AT1 4 x AT1
Ligand SO4 4 x SO4
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 65.97Å b: 89.06Å c: 194.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.245
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Glutamate receptor ion channels: structure, regulation, and function.
Traynelis et al. (2010)
14 more

7 mentions without citation

Size matters in activation/inhibition of ligand-gated ion channels.
Du et al. (2012)
6 more