9OBU
glycine/glutamate and Mg2+-bound GluN1a/2B NMDAR
Summary for 9OBU
| Entry DOI | 10.2210/pdb9obu/pdb |
| EMDB information | 70299 |
| Descriptor | Glutamate receptor ionotropic, NMDA 1, Glutamate receptor ionotropic, NMDA 2B (2 entities in total) |
| Functional Keywords | membrane proteins, ion channel, nmdar, membrane protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 4 |
| Total formula weight | 383449.72 |
| Authors | Steigerwald, R.,Furukawa, H. (deposition date: 2025-04-23, release date: 2026-05-06, Last modification date: 2026-06-24) |
| Primary citation | Steigerwald, R.,Epstein, M.,Chou, T.H.,Simorowski, N.,Furukawa, H. Molecular mechanism of calcium permeability and magnesium block in NMDA receptors. Nat.Neurosci., 29:1293-1302, 2026 Cited by PubMed Abstract: Hebbian neuroplasticity, which is thought to be a cellular substrate of learning and memory, can occur by means of coincidental detection of presynaptic neurotransmitter release and Ca influx upon postsynaptic depolarization. This is mediated at a molecular level by N-methyl-D-aspartate-type glutamate receptors, which bind glutamate and glycine and facilitate Ca influx upon relief of Mg channel block during membrane depolarization. However, the structural mechanism underlying Ca permeability and Mg blockade in N-methyl-D-aspartate-type glutamate receptors has yet to be fully elucidated. Here we demonstrate using single-particle cryo-electron microscopy that Ca permeation through the narrow constriction of the cation selectivity filter involves partial dehydration, as evidenced by several Ca binding sites. In contrast, Mg binds outside of the selectivity filter through a water network and remains hydrated, thereby acting as a channel blocker. Furthermore, the lipid network around the selectivity filter influences the stability of Mg binding in a voltage-dependent manner. Our study details the transmembrane chemistry essential for initiating neuroplasticity. PubMed: 42086762DOI: 10.1038/s41593-026-02283-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.16 Å) |
Structure validation
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