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9OBV

Mg2+-bound GluN1a/2B NMDAR (upper)

Summary for 9OBV
Entry DOI10.2210/pdb9obv/pdb
EMDB information70300
DescriptorGlutamate receptor ionotropic, NMDA 1, Glutamate receptor ionotropic, NMDA 2B, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, ... (5 entities in total)
Functional Keywordsmembrane protein, ion channels, nmdar
Biological sourceRattus norvegicus (Norway rat)
More
Total number of polymer chains4
Total formula weight386514.33
Authors
Steigerwald, R.,Furukawa, H. (deposition date: 2025-04-23, release date: 2026-05-06, Last modification date: 2026-06-24)
Primary citationSteigerwald, 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: 42086762
DOI: 10.1038/s41593-026-02283-3
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.21 Å)
Structure validation

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PDB entries from 2026-06-24

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