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 mechanism of glutamate receptor activation and desensitization.
Journal, issue, pages	Nature, Vol. 514, Issue 7522, Page 328-334, Year 2014
Publish date	Oct 16, 2014
Authors	Joel R Meyerson / Janesh Kumar / Sagar Chittori / Prashant Rao / Jason Pierson / Alberto Bartesaghi / Mark L Mayer / Sriram Subramaniam /
PubMed Abstract	Ionotropic glutamate receptors are ligand-gated ion channels that mediate excitatory synaptic transmission in the vertebrate brain. To gain a better understanding of how structural changes gate ion ...Ionotropic glutamate receptors are ligand-gated ion channels that mediate excitatory synaptic transmission in the vertebrate brain. To gain a better understanding of how structural changes gate ion flux across the membrane, we trapped rat AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid) and kainate receptor subtypes in their major functional states and analysed the resulting structures using cryo-electron microscopy. We show that transition to the active state involves a 'corkscrew' motion of the receptor assembly, driven by closure of the ligand-binding domain. Desensitization is accompanied by disruption of the amino-terminal domain tetramer in AMPA, but not kainate, receptors with a two-fold to four-fold symmetry transition in the ligand-binding domains in both subtypes. The 7.6 Å structure of a desensitized kainate receptor shows how these changes accommodate channel closing. These findings integrate previous physiological, biochemical and structural analyses of glutamate receptors and provide a molecular explanation for key steps in receptor gating.
External links	Nature / PubMed:25119039 / PubMed Central
Methods	EM (single particle)
Resolution	7.6 - 25.9 Å
Structure data	2680 4uqj EMDB-2680: Density map of GluA2em in complex with ZK200775 PDB-4uqj: Cryo-EM density map of GluA2em in complex with ZK200775 Method: EM (single particle) / Resolution: 10.4 Å 2684 4uq6 EMDB-2684: Density map of GluA2em in complex with LY451646 and glutamate PDB-4uq6: Electron density map of GluA2em in complex with LY451646 and glutamate Method: EM (single particle) / Resolution: 12.8 Å 2685 4uqq EMDB-2685: Density map of GluK2 desensitized state in complex with 2S,4R-4-methylglutamate PDB-4uqq: Electron density map of GluK2 desensitized state in complex with 2S,4R-4-methylglutamate Method: EM (single particle) / Resolution: 7.6 Å EMDB-2686: Density map of GluA2em desensitized state in complex with quisqualate (class 1) Method: EM (single particle) / Resolution: 21.4 Å EMDB-2687: Density map of GluA2em desensitized state in complex with quisqualate (class 2) Method: EM (single particle) / Resolution: 25.9 Å EMDB-2688: Density map of GluA2em desensitized state in complex with quisqualate (class 3) Method: EM (single particle) / Resolution: 22.9 Å 2689 4uqk EMDB-2689: Density map of GluA2em in complex with quisqualate and LY451646 PDB-4uqk: Electron density map of GluA2em in complex with quisqualate and LY451646 Method: EM (single particle) / Resolution: 16.4 Å
Chemicals	ChemComp-GLU: GLUTAMIC ACID ChemComp-ZK1: {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid / antagonist, medicationYM ChemComp-QUS: (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID / agonistYM
Source	rattus norvegicus (Norway rat) synthetic construct (others)
Keywords	TRANSPORT PROTEIN / MEMBRANE PROTEIN / ION CHANNEL / GLUA2EM ANTAGONIST-BOUND CLOSED STATE / GLUA2EM RESTORED ACTIVE STATE