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PDBsum entry 4kcd
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Membrane protein
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PDB id
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4kcd
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References listed in PDB file
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Key reference
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Title
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Conformational analysis of nmda receptor glun1, Glun2, And glun3 ligand-Binding domains reveals subtype-Specific characteristics.
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Authors
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Y.Yao,
J.Belcher,
A.J.Berger,
M.L.Mayer,
A.Y.Lau.
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Ref.
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Structure, 2013,
21,
1788-1799.
[DOI no: ]
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PubMed id
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Abstract
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The NMDA receptor family of glutamate receptor ion channels is formed by
obligate heteromeric assemblies of GluN1, GluN2, and GluN3 subunits. GluN1 and
GluN3 bind glycine, whereas GluN2 binds glutamate. Crystal structures of the
GluN1 and GluN3A ligand-binding domains (LBDs) in their apo states unexpectedly
reveal open- and closed-cleft conformations, respectively, with water molecules
filling the binding pockets. Computed conformational free energy landscapes for
GluN1, GluN2A, and GluN3A LBDs reveal that the apo-state LBDs sample
closed-cleft conformations, suggesting that their agonists bind via a
conformational selection mechanism. By contrast, free energy landscapes for
the AMPA receptor GluA2 LBD suggest binding of glutamate via an induced-fit
mechanism. Principal component analysis reveals a rich spectrum of hinge
bending, rocking, twisting, and sweeping motions that are different for the
GluN1, GluN2A, GluN3A, and GluA2 LBDs. This variation highlights the structural
complexity of signaling by glutamate receptor ion channels.
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