6WHS
GluN1b-GluN2B NMDA receptor in non-active 1 conformation at 3.95 angstrom resolution
Summary for 6WHS
| Entry DOI | 10.2210/pdb6whs/pdb |
| Related | 6WHR 6WHT 6WHU 6WHV 6WHW 6WHX 6WHY 6WI0 6WI1 |
| EMDB information | 21673 21674 21675 21676 21677 21678 21679 21680 21681 21682 |
| Descriptor | Glutamate receptor ionotropic, NMDA 1, Glutamate receptor ionotropic, NMDA 2B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | nmdars, ligand-gated ion channels, metal transport, ionotropic glutamate receptor, membrane protein |
| Biological source | Rattus norvegicus (Rat) More |
| Total number of polymer chains | 4 |
| Total formula weight | 416481.45 |
| Authors | Chou, T.,Tajima, N.,Furukawa, H. (deposition date: 2020-04-08, release date: 2020-08-05, Last modification date: 2024-10-16) |
| Primary citation | Chou, T.H.,Tajima, N.,Romero-Hernandez, A.,Furukawa, H. Structural Basis of Functional Transitions in Mammalian NMDA Receptors. Cell, 182:357-371.e13, 2020 Cited by PubMed Abstract: Excitatory neurotransmission meditated by glutamate receptors including N-methyl-D-aspartate receptors (NMDARs) is pivotal to brain development and function. NMDARs are heterotetramers composed of GluN1 and GluN2 subunits, which bind glycine and glutamate, respectively, to activate their ion channels. Despite importance in brain physiology, the precise mechanisms by which activation and inhibition occur via subunit-specific binding of agonists and antagonists remain largely unknown. Here, we show the detailed patterns of conformational changes and inter-subunit and -domain reorientation leading to agonist-gating and subunit-dependent competitive inhibition by providing multiple structures in distinct ligand states at 4 Å or better. The structures reveal that activation and competitive inhibition by both GluN1 and GluN2 antagonists occur by controlling the tension of the linker between the ligand-binding domain and the transmembrane ion channel of the GluN2 subunit. Our results provide detailed mechanistic insights into NMDAR pharmacology, activation, and inhibition, which are fundamental to the brain physiology. PubMed: 32610085DOI: 10.1016/j.cell.2020.05.052 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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