› 3bfu

X-ray diffraction
1.95Å resolution

Structure of the ligand-binding core of GluR2 in complex with the agonist (R)-TDPA at 1.95 A resolution

Released:
DOI: 10.2210/pdb3bfu/pdb
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PDB entry 3bfu coloured by chain, front view.
PDB entry 3bfu coloured by chain, side view.
PDB entry 3bfu coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structures of the ligand-binding core of iGluR2 in complex with the agonists (R)- and (S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propionic acid explain their unusual equipotency.
Beich-Frandsen M, Pickering DS, Mirza O, Johansen TN, Greenwood J, Vestergaard B, Schousboe A, Gajhede M, Liljefors T, Kastrup JS
J Med Chem 51 1459-63 (2008)
PMID: 18269227

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
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

1 bound ligand:
Ligand R2P 4 x R2P
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P2
Unit cell:
a: 104.75Å b: 47.52Å c: 124.33Å
α: 90° β: 113.54° γ: 90°
R-values:
R R work R free
0.2 0.2 0.233
Expression system: Escherichia coli

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Citations

1 review citation

Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators.
Pøhlsgaard et al. (2011)
1 other article

1 mention without citation

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

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