4TLL
Crystal structure of GluN1/GluN2B NMDA receptor, structure 1
Summary for 4TLL
| Entry DOI | 10.2210/pdb4tll/pdb |
| Related | 4TLM |
| Descriptor | receptor subunit GluN1, receptor subunit GluN2B, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | neurotransmitter receptor, nmda receptor, glun1/glun2b, membrane protein, ion channel, signaling protein |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 4 |
| Total formula weight | 373445.55 |
| Authors | Gouaux, E.,Lee, C.-H.,Lu, W. (deposition date: 2014-05-30, release date: 2014-07-02, Last modification date: 2023-12-27) |
| Primary citation | Lee, C.H.,Lu, W.,Michel, J.C.,Goehring, A.,Du, J.,Song, X.,Gouaux, E. NMDA receptor structures reveal subunit arrangement and pore architecture. Nature, 511:191-197, 2014 Cited by PubMed Abstract: 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 ∼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. PubMed: 25008524DOI: 10.1038/nature13548 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.59 Å) |
Structure validation
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