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TitleA Binding Site Tyrosine Shapes Desensitization Kinetics and Agonist Potency at GluR2: a mutagenic, kinetic, and crystallographic study
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 35469-35476, Year 2005
Publish dateAug 11, 2005 (structure data deposition date)
AuthorsHolm, M.M. / Naur, P. / Vestergaard, B. / Geballe, M.T. / Gajhede, M. / Kastrup, J.S. / Traynelis, S.F. / Egebjerg, J.
External linksJ. Biol. Chem. / PubMed:16103115
MethodsX-ray diffraction
Resolution2.1 Å
Structure data

PDB-2anj:
Crystal Structure of the Glur2 Ligand Binding Core (S1S2J-Y450W) Mutant in Complex With the Partial Agonist Kainic Acid at 2.1 A Resolution
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-KAI:
3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE / neurotransmitter, agonist*YM

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / Ionotropic Glutamate Receptor / GluR2 Ligand-Binding Core / Agonist Complex / Mutant

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