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Structure paper

TitleStructural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating.
Journal, issue, pagesJ. Neurosci., Vol. 28, Page 932-943, Year 2008
Publish dateOct 29, 2007 (structure data deposition date)
AuthorsZhang, W. / Cho, Y. / Lolis, E. / Howe, J.R.
External linksJ. Neurosci. / PubMed:18216201
MethodsX-ray diffraction
Resolution1.7 - 2.1 Å
Structure data

PDB-3b6q:
Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) Mutant T686A in Complex with Glutamate at 2.0 Resolution
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3b6t:
Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) T686A Mutant in Complex with Quisqualate at 2.1 Resolution
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3b6w:
Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) T686S Mutant in Complex with Glutamate at 1.7 Resolution
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-HOH:
WATER

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

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / GLUR2 / T686A / MUTANT / AMPA RECEPTOR / IONOTROPIC GLUTAMATE RECEPTOR / Alternative splicing / Cell junction / Glycoprotein / Ion transport / Ionic channel / Lipoprotein / Membrane / Palmitate / Phosphorylation / Postsynaptic cell membrane / RNA editing / Synapse / Transmembrane / Transport / QUISQUALATE / T686S

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