› 9b67

Electron Microscopy
3.39Å resolution

GluA2 flip Q in complex with TARPgamma2 at pH8, class1, structure of LBD-TMD-TARPgamma2

Released:
DOI: 10.2210/pdb9b67/pdb
PDB entry 9b67 coloured by chain, front view.
PDB entry 9b67 coloured by chain, side view.
PDB entry 9b67 coloured by chain, top view.
Source organisms:
Primary publication:
Proton-triggered rearrangement of the AMPA receptor N-terminal domains impacts receptor kinetics and synaptic localization.
Ivica J, Kejzar N, Ho H, Stockwell I, Kuchtiak V, Scrutton AM, Nakagawa T, Greger IH
Nat Struct Mol Biol (2024)
PMID: 39138332
Related structures: EMD-44248

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-271877 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Voltage-dependent calcium channel gamma-2 subunit Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 323 amino acids
Theoretical weight: 35.94 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: O88602 (Residues: 1-323; Coverage: 100%)
Gene names: Cacng2, Stg
Sequence domains: PMP-22/EMP/MP20/Claudin family
Glutamate receptor 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 889 amino acids
Theoretical weight: 99.62 KDa
Source organism: Rattus norvegicus
Expression system: Homo sapiens
UniProt:
  • Canonical: P19491 (Residues: 1-868, 870-883; Coverage: 100%)
  • Best match: P19491-2 (Residues: 1-868, 870-883)
Gene names: GluA2, Glur2, Gria2
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.39Å
Relevant EMDB volumes: EMD-44248
Expression system: Homo sapiens

Quick links

Citations

1 citations in other articles

Proton-triggered rearrangement of the AMPA receptor N-terminal domains impacts receptor kinetics and synaptic localization.
Ivica et al. (2024)