3JPW

Crystal structure of amino terminal domain of the NMDA receptor subunit NR2B

Summary for 3JPW

• Entry DOI: 10.2210/pdb3jpw/pdb
• Related: 3JPY
• Descriptor: Glutamate [NMDA] receptor subunit epsilon-2, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: nmda receptor, amino terminal domain, phenylethanolamine, cell junction, cell membrane, glycoprotein, ion transport, ionic channel, magnesium, membrane, phosphoprotein, postsynaptic cell membrane, receptor, synapse, transmembrane, transport, transport protein
• Biological source: Rattus norvegicus (brown rat,rat,rats)
• Total number of polymer chains: 1
• Total formula weight: 42348.93

Authors

Karakas, E.,Simorowski, N.,Furukawa, H. (deposition date: 2009-09-04, release date: 2009-12-08, Last modification date: 2024-10-30)

Primary citation

Karakas, E.,Simorowski, N.,Furukawa, H.
Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit.
Embo J., 28:3910-3920, 2009

PubMed 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.

PubMed: 19910922
DOI: 10.1038/emboj.2009.338

Experimental method

X-RAY DIFFRACTION (2.803 Å)