› 1p1q

X-ray diffraction
2Å resolution

Crystal structure of the GluR2 ligand binding core (S1S2J) L650T mutant in complex with AMPA

Released:
DOI: 10.2210/pdb1p1q/pdb
PDB 1p1q coloured by chain and viewed from the front.
PDB 1p1q coloured by chain and viewed from the side.
PDB 1p1q coloured by chain and viewed from the top.
Source organism: Rattus norvegicus
Primary publication:
Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes.
Armstrong N, Mayer M, Gouaux E
Proc. Natl. Acad. Sci. U.S.A. 100 5736-41 (2003)
PMID: 12730367

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate receptor 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 263 amino acids
Theoretical weight: 29.21 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P19491 (Residues: 413-527, 653-796; Coverage: 30%)
Gene names: Glur2, Gria2
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand ZN 5 x ZN
Ligand AMQ 3 x AMQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21212
Unit cell:
a: 113.942Å b: 163.642Å c: 47.116Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.256 0.217 0.27
Expression system: Escherichia coli BL21

Quick links

Citations

17 review citations

Never at rest: insights into the conformational dynamics of ion channels from cryo-electron microscopy.
Lau et al. (2018)
16 more

1 mention without citation

Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes.
Armstrong et al. (2003)