RGD Reference Report - Crystal structure of a heterotetrameric NMDA receptor ion channel. - Rat Genome Database

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Crystal structure of a heterotetrameric NMDA receptor ion channel.

Authors: Karakas, Erkan  Furukawa, Hiro 
Citation: Karakas E and Furukawa H, Science. 2014 May 30;344(6187):992-7. doi: 10.1126/science.1251915.
RGD ID: 13432263
Pubmed: (View Article at PubMed) PMID:24876489
DOI: Full-text: DOI:10.1126/science.1251915

N-Methyl-D-aspartate (NMDA) receptors belong to the family of ionotropic glutamate receptors, which mediate most excitatory synaptic transmission in mammalian brains. Calcium permeation triggered by activation of NMDA receptors is the pivotal event for initiation of neuronal plasticity. Here, we show the crystal structure of the intact heterotetrameric GluN1-GluN2B NMDA receptor ion channel at 4 angstroms. The NMDA receptors are arranged as a dimer of GluN1-GluN2B heterodimers with the twofold symmetry axis running through the entire molecule composed of an amino terminal domain (ATD), a ligand-binding domain (LBD), and a transmembrane domain (TMD). The ATD and LBD are much more highly packed in the NMDA receptors than non-NMDA receptors, which may explain why ATD regulates ion channel activity in NMDA receptors but not in non-NMDA receptors.



Gene Ontology Annotations    

Biological Process

Cellular Component

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Grin1  (glutamate ionotropic receptor NMDA type subunit 1)
Grin2b  (glutamate ionotropic receptor NMDA type subunit 2B)


Additional Information