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  Subunit-specific block of cloned NMDA receptors by argiotoxin636

Raditsch, M., Ruppersberg, J. P., Kuner, T., Günther, W., Schöpfer, R., Seeburg, P. H., et al. (1993). Subunit-specific block of cloned NMDA receptors by argiotoxin636. FEBS Letters, 324(1), 63-66. doi:10.1016/0014-5793(93)81533-6.

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FEBSLett_324_1993_63.pdf (beliebiger Volltext), 396KB
 
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 Urheber:
Raditsch, Martin1, Autor           
Ruppersberg, J. Peter1, Autor           
Kuner, Thomas1, 2, 3, 4, 5, Autor           
Günther, Willy1, Autor           
Schöpfer, Ralf5, Autor           
Seeburg, Peter H.5, Autor           
Jahn, Werner6, 7, Autor           
Witzemann, Veit1, 5, 8, 9, Autor           
Affiliations:
1Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              
2Interdisciplinary WIN-Research Group on Olfactory Dynamics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497717              
3Synaptic Transmission MNTB, Max Planck Institute for Medical Research, Max Planck Society, ou_1497745              
4Synaptic Transmission, Max Planck Institute for Medical Research, Max Planck Society, ou_1497744              
5Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
6Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
7Muscle Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497731              
8Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society, ou_1497748              
9Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society, ou_1497727              

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Schlagwörter: NMDA receptor; Recombinant; Argiotoxin; Site-directed mutagenesis
 Zusammenfassung: Cloned NMDA receptor channels of the NR1-NR2A, NR1-NR2B and NR1-NR2C type show differences in argiotoxin636 block. Mutations of an asparagine residue located at a homologous position in the TM2 region of all NMDA receptor subunits, which corresponds to the Q/R site of the AMPA receptors, alters the argiotoxin636-induced block. The results suggest that the toxin interacts at this amino acid position with the putative pore forming TM2 region of the NMDA receptor subunits. Sequence differences in the TM2 segment of NR2A and NR2C subunits are not responsible for the subtype-specific sensitivity to argiotoxin636 as revealed by site-directed mutagenesis.

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Sprache(n): eng - English
 Datum: 1993-03-231993-04-132001-11-121993-06-07
 Publikationsstatus: Erschienen
 Seiten: 4
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 666804
DOI: 10.1016/0014-5793(93)81533-6
 Art des Abschluß: -

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Titel: FEBS Letters
  Andere : FEBS Lett.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Amsterdam : Elsevier
Seiten: - Band / Heft: 324 (1) Artikelnummer: - Start- / Endseite: 63 - 66 Identifikator: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501