Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specific receptor assembly.

doi:10.1074/jbc.M408413200

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Article

Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specific receptor assembly.

The Journal of biological chemistry - 15 Apr 2005

Ayalon Gai, Segev Eitan, Elgavish Sharona, Stern-Bach Yael

Abstract excerpt

The N-terminal domain (NTD) of alpha-amino-3-hydroxy-5-methylisoxazolepropionate (AMPA) and kainate glutamate receptors plays an important role in controlling subtype specific receptor assembly. To identify NTD subdomains involved in this process we generated AMPA glutamate receptor 3 (GluR3) mutants having intra-NTD substitutions with the corresponding regions of the kainate receptor GluR6 and tested their...

Topics

Alanine
Amino Acid Sequence
Animals
Blotting, Western
Cell Membrane
Cysteine
Dimerization
Dose-Response Relationship, Drug
Electrophysiology
Gene Deletion
Immunoprecipitation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mice

Models, Molecular

Molecular Sequence Data

Mutation

Oocytes

Phenotype

Protein Binding

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Open in PubMed

Identifiers

PMID: 15703162
DOI: 10.1074/jbc.M408413200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-15703162-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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