Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit

Karakas, E., Simorowski, N., Furukawa, H. (2009) Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit. Embo Journal, 28 (24). pp. 3910-3920. ISSN 0261-4189

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URL: http://www.ncbi.nlm.nih.gov/pubmed/19910922
DOI: 10.1038/emboj.2009.338

Abstract

N-methyl-D-aspartate (NMDA) receptors belong to the family of ionotropic glutamate receptors (iGluRs) that mediate the majority of fast excitatory synaptic transmission in the mammalian brain. One of the hallmarks for the function of NMDA receptors is that their ion channel activity is allosterically regulated by binding of modulator compounds to the extracellular amino-terminal domain (ATD) distinct from the L-glutamate-binding domain. The molecular basis for the ATD-mediated allosteric regulation has been enigmatic because of a complete lack of structural information on NMDA receptor ATDs. Here, we report the crystal structures of ATD from the NR2B NMDA receptor subunit in the zinc-free and zinc-bound states. The structures reveal the overall clamshell-like architecture distinct from the non-NMDA receptor ATDs and molecular determinants for the zinc-binding site, ion-binding sites, and the architecture of the putative phenylethanolamine-binding site.

Item Type: Paper
Uncontrolled Keywords: allosteric inhibition crystallography NMDA receptor zinc binding
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > NMDA receptor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL Post Doctoral Fellows
CSHL labs > Furukawa lab
Depositing User: Leigh Johnson
Date Deposited: 26 Mar 2012 18:01
Last Modified: 08 Sep 2017 16:01
PMCID: PMC2797058
Related URLs:
Dataset ID:
URI: http://repository.cshl.edu/id/eprint/25161

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