4TLM: Crystal Structure Of Glun1/glun2b Nmda Receptor, Structure 2

N-methyl-d-aspartate (NMDA) receptors are Hebbian-like coincidence detectors, requiring binding of glycine and glutamate in combination with the relief of voltage-dependent magnesium block to open an ion conductive pore across the membrane bilayer. Despite the importance of the NMDA receptor in the development and function of the brain, a molecular structure of an intact receptor has remained elusive. Here we present X-ray crystal structures of the Xenopus laevis GluN1-GluN2B NMDA receptor with the allosteric inhibitor, Ro25-6981, partial agonists and the ion channel blocker, MK-801. Receptor subunits are arranged in a 1-2-1-2 fashion, demonstrating extensive interactions between the amino-terminal and ligand-binding domains. The transmembrane domains harbour a closed-blocked ion channel, a pyramidal central vestibule lined by residues implicated in binding ion channel blockers and magnesium, and a approximately twofold symmetric arrangement of ion channel pore loops. These structures provide new insights into the architecture, allosteric coupling and ion channel function of NMDA receptors.
PDB ID: 4TLMDownload
MMDB ID: 121413
PDB Deposition Date: 2014/5/30
Updated in MMDB: 2014/10
Experimental Method:
x-ray diffraction
Resolution: 3.77  Å
Source Organism:
Similar Structures:
Biological Unit for 4TLM: tetrameric; determined by author and by software (PISA)
Molecular Components in 4TLM
Label Count Molecule
Proteins (4 molecules)
Receptor Subunit Glun1
Molecule annotation
Receptor Subunit Glun2b(Gene symbol: nr2b)
Molecule annotation
Chemicals (11 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB