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TitleStructural mechanism of glutamate receptor activation and desensitization.
Journal, issue, pagesNature, Vol. 514, Issue 7522, Page 328-334, Year 2014
Publish dateOct 16, 2014
AuthorsJoel R Meyerson / Janesh Kumar / Sagar Chittori / Prashant Rao / Jason Pierson / Alberto Bartesaghi / Mark L Mayer / Sriram Subramaniam /
PubMed AbstractIonotropic 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 linksNature / PubMed:25119039 / PubMed Central
MethodsEM (single particle)
Resolution7.6 - 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 / Glutamic acid

ChemComp-ZK1:
{[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid / antagonist, medication*YM / Fanapanel

ChemComp-QUS:
(S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID / agonist*YM / Quisqualic acid

Source
  • rattus norvegicus (Norway rat)
  • synthetic construct (others)
KeywordsTRANSPORT PROTEIN / MEMBRANE PROTEIN / ION CHANNEL / GLUA2EM ANTAGONIST-BOUND CLOSED STATE / GLUA2EM RESTORED ACTIVE STATE

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