› 1syi

X-ray diffraction
2.1Å resolution

X-RAY STRUCTURE OF THE Y702F MUTANT OF THE GLUR2 LIGAND-BINDING CORE (S1S2J) IN COMPLEX WITH (S)-CPW399 AT 2.1 A RESOLUTION.

Released:
DOI: 10.2210/pdb1syi/pdb
PDB entry 1syi coloured by chain, front view.
PDB entry 1syi coloured by chain, side view.
PDB entry 1syi coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Tyr702 is an important determinant of agonist binding and domain closure of the ligand-binding core of GluR2.
Frandsen A, Pickering DS, Vestergaard B, Kasper C, Nielsen BB, Greenwood JR, Campiani G, Fattorusso C, Gajhede M, Schousboe A, Kastrup JS
Mol Pharmacol 67 703-13 (2005)
PMID: 15591246

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
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 29.21 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19491 (Residues: 413-796; Coverage: 30%)
Gene names: GluA2, Glur2, Gria2
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

1 bound ligand:
Ligand CPW 2 x CPW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P41
Unit cell:
a: 47.719Å b: 47.719Å c: 237.401Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.254
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

3 mentions without citation

Enhanced efficacy without further cleft closure: reevaluating twist as a source of agonist efficacy in AMPA receptors.
Birdsey-Benson et al. (2010)
2 more