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 basis of kainate subtype glutamate receptor desensitization.
Journal, issue, pages	Nature, Vol. 537, Issue 7621, Page 567-571, Year 2016
Publish date	Sep 22, 2016
Authors	Joel R Meyerson / Sagar Chittori / Alan Merk / Prashant Rao / Tae Hee Han / Mihaela Serpe / Mark L Mayer / Sriram Subramaniam /
PubMed Abstract	Glutamate receptors are ligand-gated tetrameric ion channels that mediate synaptic transmission in the central nervous system. They are instrumental in vertebrate cognition and their dysfunction ...Glutamate receptors are ligand-gated tetrameric ion channels that mediate synaptic transmission in the central nervous system. They are instrumental in vertebrate cognition and their dysfunction underlies diverse diseases. In both the resting and desensitized states of AMPA and kainate receptor subtypes, the ion channels are closed, whereas the ligand-binding domains, which are physically coupled to the channels, adopt markedly different conformations. Without an atomic model for the desensitized state, it is not possible to address a central problem in receptor gating: how the resting and desensitized receptor states both display closed ion channels, although they have major differences in the quaternary structure of the ligand-binding domain. Here, by determining the structure of the kainate receptor GluK2 subtype in its desensitized state by cryo-electron microscopy (cryo-EM) at 3.8 Å resolution, we show that desensitization is characterized by the establishment of a ring-like structure in the ligand-binding domain layer of the receptor. Formation of this 'desensitization ring' is mediated by staggered helix contacts between adjacent subunits, which leads to a pseudo-four-fold symmetric arrangement of the ligand-binding domains, illustrating subtle changes in symmetry that are important for the gating mechanism. Disruption of the desensitization ring is probably the key switch that enables restoration of the receptor to its resting state, thereby completing the gating cycle.
External links	Nature / PubMed:27580033 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.271 - 11.6 Å
Structure data	8289 5kuf EMDB-8289, PDB-5kuf: GluK2EM with 2S,4R-4-methylglutamate Method: EM (single particle) / Resolution: 3.8 Å 8290 5kuh EMDB-8290, PDB-5kuh: GluK2EM with LY466195 Method: EM (single particle) / Resolution: 11.6 Å PDB-5cmk: Crystal structure of the GluK2EM LBD dimer assembly complex with glutamate and LY466195 Method: X-RAY DIFFRACTION / Resolution: 1.801 Å PDB-5cmm: Crystal structure of the GluK2EM LBD dimer assembly complex with 2S,4R-4-methylglutamate Method: X-RAY DIFFRACTION / Resolution: 1.271 Å
Chemicals	ChemComp-GLU: GLUTAMIC ACID ChemComp-LI: Unknown entry ChemComp-CL: Unknown entry ChemComp-LY5: (3S,4aR,6S,8aR)-6-{[(2S)-2-carboxy-4,4-difluoropyrrolidin-1-yl]methyl}decahydroisoquinoline-3-carboxylic acid ChemComp-SO4: SULFATE ION ChemComp-HOH: WATER ChemComp-SYM: 2S,4R-4-METHYLGLUTAMATE
Source	rattus norvegicus (Norway rat) homo sapiens (human)
Keywords	TRANSPORT PROTEIN / Membrane protein / SIGNALING PROTEIN / GluK2EM with 2S / 4R-4-methylglutamate / GluK2EM with LY466195