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Structure paper

TitleMechanism of NMDA Receptor Inhibition and Activation.
Journal, issue, pagesCell, Vol. 165, Issue 3, Page 704-714, Year 2016
Publish dateApr 21, 2016
AuthorsShujia Zhu / Richard A Stein / Craig Yoshioka / Chia-Hsueh Lee / April Goehring / Hassane S Mchaourab / Eric Gouaux /
PubMed AbstractN-methyl-D-aspartate receptors (NMDARs) are glutamate-gated, calcium-permeable ion channels that mediate synaptic transmission and underpin learning and memory. NMDAR dysfunction is directly ...N-methyl-D-aspartate receptors (NMDARs) are glutamate-gated, calcium-permeable ion channels that mediate synaptic transmission and underpin learning and memory. NMDAR dysfunction is directly implicated in diseases ranging from seizure to ischemia. Despite its fundamental importance, little is known about how the NMDAR transitions between inactive and active states and how small molecules inhibit or activate ion channel gating. Here, we report electron cryo-microscopy structures of the GluN1-GluN2B NMDA receptor in an ensemble of competitive antagonist-bound states, an agonist-bound form, and a state bound with agonists and the allosteric inhibitor Ro25-6981. Together with double electron-electron resonance experiments, we show how competitive antagonists rupture the ligand binding domain (LBD) gating "ring," how agonists retain the ring in a dimer-of-dimers configuration, and how allosteric inhibitors, acting within the amino terminal domain, further stabilize the LBD layer. These studies illuminate how the LBD gating ring is fundamental to signal transduction and gating in NMDARs.
External linksCell / PubMed:27062927 / PubMed Central
MethodsEM (single particle)
Resolution7.0 - 15.4 Å
Structure data

EMDB-8097, PDB-5iou:
Cryo-EM structure of GluN1/GluN2B NMDA receptor in the glutamate/glycine-bound conformation
Method: EM (single particle) / Resolution: 7.0 Å

EMDB-8098, PDB-5iov:
Cryo-EM structure of GluN1/GluN2B NMDA receptor in the glutamate/glycine/Ro25-6981-bound conformation
Method: EM (single particle) / Resolution: 7.5 Å

EMDB-8101, PDB-5ipq:
Cryo-EM structure of GluN1/GluN2B NMDA receptor in the DCKA/D-APV-bound conformation, state 2
Method: EM (single particle) / Resolution: 13.5 Å

EMDB-8102, PDB-5ipr:
Cryo-EM structure of GluN1/GluN2B NMDA receptor in the DCKA/D-APV-bound conformation, state 3
Method: EM (single particle) / Resolution: 14.1 Å

EMDB-8103, PDB-5ips:
Cryo-EM structure of GluN1/GluN2B NMDA receptor in the DCKA/D-APV-bound conformation, state 4
Method: EM (single particle) / Resolution: 13.5 Å

EMDB-8104, PDB-5ipt:
Cryo-EM structure of GluN1/GluN2B NMDA receptor in the DCKA/D-APV-bound conformation, state 5
Method: EM (single particle) / Resolution: 14.1 Å

EMDB-8105, PDB-5ipu:
Cryo-EM structure of GluN1/GluN2B NMDA receptor in the DCKA/D-APV-bound conformation, state 6
Method: EM (single particle) / Resolution: 15.4 Å

EMDB-8106, PDB-5ipv:
Cryo-EM structure of GluN1/GluN2B NMDA receptor in the DCKA/D-APV-bound conformation, state 1
Method: EM (single particle) / Resolution: 9.25 Å

Chemicals

ChemComp-GLY:
GLYCINE

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-QEM:
4-[(1R,2S)-3-(4-benzylpiperidin-1-yl)-1-hydroxy-2-methylpropyl]phenol

Source
  • xenopus laevis (African clawed frog)
KeywordsSIGNALING PROTEIN / ligand-gated ion channel / synaptic transmission

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