1PB8

CRYSTAL STRUCTURE OF THE NR1 LIGAND BINDING CORE IN COMPLEX WITH D-SERINE AT 1.45 ANGSTROMS RESOLUTION

Summary for 1PB8

• Entry DOI: 10.2210/pdb1pb8/pdb
• Related: 1PB7 1PB9
• Descriptor: N-methyl-D-aspartate Receptor Subunit 1, D-SERINE (3 entities in total)
• Functional Keywords: ligand binding receptor; rat; nr1, ligand binding protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cell membrane ; Multi-pass membrane protein : P35439
• Total number of polymer chains: 1
• Total formula weight: 33432.13

Authors

Furukawa, H.,Gouaux, E. (deposition date: 2003-05-14, release date: 2003-06-24, Last modification date: 2017-07-26)

Primary citation

Furukawa, H.,Gouaux, E.
Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core
Embo J., 22:2873-2885, 2003

PubMed Abstract: Excitatory neurotransmission mediated by the N-methyl-D-aspartate subtype of ionotropic glutamate receptors is fundamental to the development and function of the mammalian central nervous system. NMDA receptors require both glycine and glutamate for activation with NR1 and NR2 forming glycine and glutamate sites, respectively. Mechanisms to describe agonist and antagonist binding, and activation and desensitization of NMDA receptors have been hampered by the lack of high-resolution structures. Here, we describe the cocrystal structures of the NR1 S1S2 ligand-binding core with the agonists glycine and D-serine (DS), the partial agonist D-cycloserine (DCS) and the antagonist 5,7-dichlorokynurenic acid (DCKA). The cleft of the S1S2 'clamshell' is open in the presence of the antagonist DCKA and closed in the glycine, DS and DCS complexes. In addition, the NR1 S1S2 structure reveals the fold and interactions of loop 1, a cysteine-rich region implicated in intersubunit allostery.

PubMed: 12805203
DOI: 10.1093/emboj/cdg303

Experimental method

X-RAY DIFFRACTION (1.45 Å)