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	Structural insights into assembly and function of GluN1-2C, GluN1-2A-2C, and GluN1-2D NMDARs.
Journal, issue, pages	Mol Cell, Vol. 82, Issue 23, Page 4548-44563.e4, Year 2022
Publish date	Dec 1, 2022
Authors	Tsung-Han Chou / Hyunook Kang / Noriko Simorowski / Stephen F Traynelis / Hiro Furukawa /
PubMed Abstract	Neurotransmission mediated by diverse subtypes of N-methyl-D-aspartate receptors (NMDARs) is fundamental for basic brain functions and development as well as neuropsychiatric diseases and disorders. ...Neurotransmission mediated by diverse subtypes of N-methyl-D-aspartate receptors (NMDARs) is fundamental for basic brain functions and development as well as neuropsychiatric diseases and disorders. NMDARs are glycine- and glutamate-gated ion channels that exist as heterotetramers composed of obligatory GluN1 and GluN2(A-D) and/or GluN3(A-B). The GluN2C and GluN2D subunits form ion channels with distinct properties and spatio-temporal expression patterns. Here, we provide the structures of the agonist-bound human GluN1-2C NMDAR in the presence and absence of the GluN2C-selective positive allosteric potentiator (PAM), PYD-106, the agonist-bound GluN1-2A-2C tri-heteromeric NMDAR, and agonist-bound GluN1-2D NMDARs by single-particle electron cryomicroscopy. Our analysis shows unique inter-subunit and domain arrangements of the GluN2C NMDARs, which contribute to functional regulation and formation of the PAM binding pocket and is distinct from GluN2D NMDARs. Our findings here provide the fundamental blueprint to study GluN2C- and GluN2D-containing NMDARs, which are uniquely involved in neuropsychiatric disorders.
External links	Mol Cell / PubMed:36309015 / PubMed Central
Methods	EM (single particle)
Resolution	3.26 - 4.24 Å
Structure data	27953 8e92 EMDB-27953, PDB-8e92: D-cycloserine and glutamate bound Human GluN1a-GluN2C NMDA receptor in intact conformation Method: EM (single particle) / Resolution: 3.96 Å 27954 8e93 EMDB-27954, PDB-8e93: D-cycloserine and glutamate bound Human GluN1a-GluN2C NMDA receptor in splayed conformation Method: EM (single particle) / Resolution: 3.71 Å 27955 8e94 EMDB-27955, PDB-8e94: PYD-106-bound Human GluN1a-GluN2C NMDA receptor in intact conformation Method: EM (single particle) / Resolution: 3.72 Å 27957 8e96 EMDB-27957, PDB-8e96: Glycine and glutamate bound Human GluN1a-GluN2D NMDA receptor Method: EM (single particle) / Resolution: 3.38 Å 27958 8e97 EMDB-27958, PDB-8e97: PYD-106-bound Human GluN1a-GluN2C NMDA receptor in splayed conformation Method: EM (single particle) / Resolution: 4.19 Å 27959 8e98 EMDB-27959, PDB-8e98: D-cycloserine and glutamate bound Human GluN1a-GluN2C NMDA receptor in nanodisc - intact conformation Method: EM (single particle) / Resolution: 3.75 Å EMDB-27960: D-cycloserine and glutamate bound Human GluN1a-GluN2C NMDA receptor in nanodisc - splayed conformation Method: EM (single particle) / Resolution: 3.28 Å 27961 8e99 EMDB-27961, PDB-8e99: Human GluN1a-GluN2A-GluN2C triheteromeric NMDA receptor in complex with Nb-4 Method: EM (single particle) / Resolution: 4.24 Å EMDB-28051: Local refined map of the LBD region of Human GluN1a-GluN2D NMDA receptor Method: EM (single particle) / Resolution: 3.26 Å EMDB-28052: Local refined map of ATD region of GluN1a-2D complex Method: EM (single particle) / Resolution: 3.9 Å EMDB-28053: Local refined map of the TMD region of Human GluN1a-GluN2D NMDA receptor Method: EM (single particle) / Resolution: 3.92 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine ChemComp-IWB: methyl 4-[(2~{R})-3-ethanoyl-1-[2-(2-methyl-1~{H}-indol-3-yl)ethyl]-4-oxidanyl-5-oxidanylidene-2~{H}-pyrrol-2-yl]benzoate ChemComp-GLY: GLYCINE / Glycine ChemComp-GLU: GLUTAMIC ACID / Glutamic acid
Source	homo sapiens (human) lama glama (llama)
Keywords	TRANSPORT PROTEIN / Ligand-gated ion channel / ionotropic glutamate receptor / synaptic protein / voltage-gate ion channel / TRANSPORT PROTEIN/IMMUNE SYSTEM / TRANSPORT PROTEIN-IMMUNE SYSTEM complex