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Journal Article

Subunit-specific block of cloned NMDA receptors by argiotoxin636

MPS-Authors
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Raditsch,  Martin
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Ruppersberg,  J. Peter
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Kuner,  Thomas
Interdisciplinary WIN-Research Group on Olfactory Dynamics, Max Planck Institute for Medical Research, Max Planck Society;
Synaptic Transmission MNTB, Max Planck Institute for Medical Research, Max Planck Society;
Synaptic Transmission, Max Planck Institute for Medical Research, Max Planck Society;
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Günther,  Willy
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Schöpfer,  Ralf
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Seeburg,  Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Jahn,  Werner
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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Witzemann,  Veit
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society;
Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-AA44-6
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.