› 2i0c

X-ray diffraction
2.25Å resolution

Crystal structure of the GluR6 ligand binding core dimer crosslinked by disulfide bonds between Y490C and L752C at 2.25 Angstroms Resolution

Released:
DOI: 10.2210/pdb2i0c/pdb
PDB entry 2i0c coloured by chain, front view.
PDB entry 2i0c coloured by chain, side view.
PDB entry 2i0c coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Conformational restriction blocks glutamate receptor desensitization.
Weston MC, Schuck P, Ghosal A, Rosenmund C, Mayer ML
Nat Struct Mol Biol 13 1120-7 (2006)
PMID: 17115050

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154585 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate receptor ionotropic, kainate 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 259 amino acids
Theoretical weight: 29.26 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P42260 (Residues: 429-544, 667-806; Coverage: 29%)
Gene names: Glur6, Grik2
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P4
Unit cell:
a: 108.79Å b: 108.79Å c: 47.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.172 0.244
Expression system: Escherichia coli

Quick links

Citations

18 review citations

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

1 mention without citation

Defining the structural relationship between kainate-receptor deactivation and desensitization.
Dawe et al. (2013)