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Structure paper

TitleStructures of the ligand-binding core of iGluR2 in complex with the agonists (R)- and (S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propionic acid explain their unusual equipotency.
Journal, issue, pagesJ. Med. Chem., Vol. 51, Page 1459-1463, Year 2008
Publish dateNov 23, 2007 (structure data deposition date)
AuthorsBeich-Frandsen, M. / Pickering, D.S. / Mirza, O. / Johansen, T.N. / Greenwood, J. / Vestergaard, B. / Schousboe, A. / Gajhede, M. / Liljefors, T. / Kastrup, J.S.
External linksJ. Med. Chem. / PubMed:18269227
MethodsX-ray diffraction
Resolution1.95 - 2.27 Å
Structure data

PDB-3bft:
Structure of the ligand-binding core of GluR2 in complex with the agonist (S)-TDPA at 2.25 A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

PDB-3bfu:
Structure of the ligand-binding core of GluR2 in complex with the agonist (R)-TDPA at 1.95 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-S2P:
(2S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid

ChemComp-ZN:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-CAC:
CACODYLATE ION

ChemComp-HOH:
WATER

ChemComp-R2P:
(2R)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / AMPA receptor / GluR2 / ligand-binding core / agonist / (S)-TDPA / Cell junction / Endoplasmic reticulum / Glycoprotein / Ion transport / Ionic channel / Lipoprotein / Membrane / Palmitate / Phosphoprotein / Postsynaptic cell membrane / RNA editing / Synapse / Transmembrane / Transport / (R)-TDPA / Alternative splicing

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