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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-AA44-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-2744-8
Genre: Journal Article

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FEBSLett_324_1993_63.pdf (Any fulltext), 396KB
 
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 Creators:
Raditsch, Martin1, Author              
Ruppersberg, J. Peter1, Author              
Kuner, Thomas1, 2, 3, 4, 5, Author              
Günther, Willy1, Author              
Schöpfer, Ralf5, Author              
Seeburg, Peter H.5, Author              
Jahn, Werner6, 7, Author              
Witzemann, Veit1, 5, 8, 9, Author              
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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Free keywords: NMDA receptor; Recombinant; Argiotoxin; Site-directed mutagenesis
 Abstract: 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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Language(s): eng - English
 Dates: 1993-03-231993-04-132001-11-121993-06-07
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666804
DOI: 10.1016/0014-5793(93)81533-6
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 324 (1) Sequence Number: - Start / End Page: 63 - 66 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501