BAIT

GRIA2

GluA2, GluR-K2, GluR2, gluR-B
glutamate receptor, ionotropic, AMPA 2
GO Process (11)
GO Function (10)
GO Component (23)
Rattus norvegicus
PREY

GRIA2

GluA2, GluR-K2, GluR2, gluR-B
glutamate receptor, ionotropic, AMPA 2
GO Process (11)
GO Function (10)
GO Component (23)
Rattus norvegicus

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity.

Lunn ML, Hogner A, Stensbol TB, Gouaux E, Egebjerg J, Kastrup JS

Two X-ray structures of the GluR2 ligand-binding core in complex with (S)-2-amino-3-(5-tert-butyl-3-hydroxy-4-isoxazolyl)propionic acid ((S)-ATPA) have been determined with and without Zn(2+) ions. (S)-ATPA induces a domain closure of ca. 21 degrees compared to the apo form. The tert-butyl moiety of (S)-ATPA is buried in a partially hydrophobic pocket and forces the ligand into the glutamate-like binding mode. The structures provide ... [more]

J Med Chem Feb. 27, 2003; 46(5);872-5 [Pubmed: 12593667]

Throughput

  • Low Throughput

Additional Notes

  • crystal structure of dimeric Gria2 in complex with a small molecule inhibitor

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
GRIA2 GRIA2
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
3673843
GRIA2 GRIA2
Co-purification
Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Low-BioGRID
-

Curated By

  • BioGRID