3OEL
Crystal structure of GluN2D ligand-binding core in complex with D-glutamate
Summary for 3OEL
| Entry DOI | 10.2210/pdb3oel/pdb |
| Related | 3OEK 3OEM 3OEN |
| Descriptor | Glutamate [NMDA] receptor subunit epsilon-4, D-GLUTAMIC ACID (3 entities in total) |
| Functional Keywords | ion channel, d-glutamate, disulfide bonds, transport protein |
| Biological source | Rattus norvegicus (brown rat,rat,rats) More |
| Cellular location | Cell membrane; Multi-pass membrane protein: Q62645 |
| Total number of polymer chains | 1 |
| Total formula weight | 32188.75 |
| Authors | Simorowski, N.,Furukawa, H. (deposition date: 2010-08-12, release date: 2011-05-11, Last modification date: 2024-11-06) |
| Primary citation | Vance, K.M.,Simorowski, N.,Traynelis, S.F.,Furukawa, H. Ligand-specific deactivation time course of GluN1/GluN2D NMDA receptors. Nat Commun, 2:294-294, 2011 Cited by PubMed Abstract: N-methyl-D-aspartate (NMDA) receptors belong to the family of ionotropic glutamate receptors that mediate a majority of excitatory synaptic transmission. One unique property of GluN1/GluN2D NMDA receptors is an unusually prolonged deactivation time course following the removal of L-glutamate. Here we show, using x-ray crystallography and electrophysiology, that the deactivation time course of GluN1/GluN2D receptors is influenced by the conformational variability of the ligand-binding domain (LBD) as well as the structure of the activating ligand. L-glutamate and L-CCG-IV induce significantly slower deactivation time courses compared with other agonists. Crystal structures of the isolated GluN2D LBD in complex with various ligands reveal that the binding of L-glutamate induces a unique conformation at the backside of the ligand-binding site in proximity to the region at which the transmembrane domain would be located in the intact receptors. These data suggest that the activity of the GluN1/GluN2D NMDA receptor is controlled distinctively by the endogenous neurotransmitter L-glutamate. PubMed: 21522138DOI: 10.1038/ncomms1295 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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