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  Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit

Ivanovic, A., Reiländer, H., Laube, B., & Kuhse, J. (1998). Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit. The Journal of Biological Chemistry, 273(32), 19933-19937. doi:10.1074/jbc.273.32.19933.

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 Urheber:
Ivanovic, Aleksandra1, Autor
Reiländer, Helmut1, Autor           
Laube, Bodo2, Autor           
Kuhse, Jochen2, Autor           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461704              

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 Zusammenfassung: Glycine is an essential co-agonist of the excitatory N-methyl-d-aspartate (NMDA) receptor, a subtype of the ionotropic glutamate receptor family. The glycine binding site of this hetero-oligomeric ion channel protein is formed by two distinct extracellular regions, S1 and S2, of the NR1 subunit, whereas the homologous domains of the NR2 subunit mediate glutamate binding. Here, segments S1 and S2 of the NR1 polypeptide were fused via a linker peptide followed by N- and C-terminally tagging with Flag and His6 epitopes, respectively. Infection of High Five insect cells with a recombinant baculovirus containing this glycine binding site construct resulted in efficient secretion of a soluble fusion protein of about 53 kDa. After affinity purification to near-homogeneity, the fusion protein bound the competitive glycine site antagonist [3H]MDL105,519 with high affinity (Kd = 5.22 ± 0.13 nm) similar to that determined with rat brain membrane fractions. This high affinity binding could be competed by the glycine site antagonist 7-chlorokynurenic acid as well as the agonists glycine and d-serine but not by l-glutamate. This indicates that the S1 and S2 domains of the NR1 subunit are sufficient for the formation of a glycine binding site that displays pharmacological properties similar to those of the NMDA receptorin vivo.

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Sprache(n): eng - English
 Datum: 1998-05-081998-03-271998-08-07
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1074/jbc.273.32.19933
PMID: 968532
 Art des Abschluß: -

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Titel: The Journal of Biological Chemistry
  Andere : JBC
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Seiten: - Band / Heft: 273 (32) Artikelnummer: - Start- / Endseite: 19933 - 19937 Identifikator: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1