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PDBsum entry 4tll
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Signaling protein
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PDB id
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4tll
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Contents |
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767 a.a.
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738 a.a.
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719 a.a.
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References listed in PDB file
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Key reference
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Title
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Nmda receptor structures reveal subunit arrangement and pore architecture.
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Authors
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C.H.Lee,
W.Lü,
J.C.Michel,
A.Goehring,
J.Du,
X.Song,
E.Gouaux.
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Ref.
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Nature, 2014,
511,
191-197.
[DOI no: ]
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PubMed id
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Abstract
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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.
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