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Structure paper

TitleSubunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors.
Journal, issue, pagesNature, Vol. 475, Page 249-253, Year 2011
Publish dateJan 20, 2011 (structure data deposition date)
AuthorsKarakas, E. / Simorowski, N. / Furukawa, H.
External linksNature / PubMed:21677647
MethodsX-ray diffraction
Resolution2.001 - 3.003 Å
Structure data

PDB-3qek:
Crystal structure of amino terminal domain of the NMDA receptor subunit GluN1
Method: X-RAY DIFFRACTION / Resolution: 2.001 Å

PDB-3qel:
Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2B in complex with ifenprodil
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3qem:
Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2B in complex with Ro 25-6981
Method: X-RAY DIFFRACTION / Resolution: 3.003 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-QEL:
4-[(1R,2S)-2-(4-benzylpiperidin-1-yl)-1-hydroxypropyl]phenol

ChemComp-QEM:
4-[(1R,2S)-3-(4-benzylpiperidin-1-yl)-1-hydroxy-2-methylpropyl]phenol

Source
  • xenopus laevis (African clawed frog)
  • rattus norvegicus (Norway rat)
KeywordsTRANSPORT PROTEIN / amino terminal domain / ion channel / NMDA receptor / allosteric modulation / phenylethanolamine / polyamine / extracellular / membrane / N-Glycosylation / transmembrane

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