Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Mechanism of NMDA Receptor Inhibition and Activation.
Journal, issue, pages	Cell, Vol. 165, Issue 3, Page 704-714, Year 2016
Publish date	Apr 21, 2016
Authors	Shujia Zhu / Richard A Stein / Craig Yoshioka / Chia-Hsueh Lee / April Goehring / Hassane S Mchaourab / Eric Gouaux /
PubMed Abstract	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 ...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 links	Cell / PubMed:27062927 / PubMed Central
Methods	EM (single particle)
Resolution	7.0 - 15.4 Å
Structure data	8097 5iou 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 8098 5iov 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 8101 5ipq 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 8102 5ipr 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 8103 5ips 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 8104 5ipt 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 8105 5ipu 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 8106 5ipv 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)
Keywords	SIGNALING PROTEIN / ligand-gated ion channel / synaptic transmission