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  Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptor

Burnashev, N., Schöpfer, R., Monyer, H., Ruppersberg, J. P., Günther, W., Seeburg, P. H., et al. (1992). Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptor. Science, 257(5075), 1415-1419. doi:10.1126/science.1382314.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-10C9-B Version Permalink: http://hdl.handle.net/21.11116/0000-0002-6012-D
Genre: Journal Article

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Burnashev, Nail1, Author              
Schöpfer, Ralf2, Author              
Monyer, Hannah2, Author              
Ruppersberg, J. Peter1, Author              
Günther, Willy1, Author              
Seeburg, Peter H.2, Author              
Sakmann, Bert1, Author              
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1Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              
2Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              

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 Abstract: The N-methyl-D-aspartate (NMDA) receptor forms a cation-selective channel with a high calcium permeability and sensitivity to channel block by extracellular magnesium. These properties, which are believed to be important for the induction of long-term changes in synaptic strength, are imparted by asparagine residues in a putative channel-forming segment of the protein, transmembrane 2 (TM2). In the NR1 subunit, replacement of this asparagine by a glutamine residue decreases calcium permeability of the channel and slightly reduces magnesium block. The same substitution in NR2 subunits strongly reduces magnesium block and increases the magnesium permeability but barely affects calcium permeability. These asparagines are in a position homologous to the site in the TM2 region (Q/R site) of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors that is occupied by either glutamine (Q) or arginine (R) and that controls divalent cation permeability of the AMPA receptor channel. Hence AMPA and NMDA receptor channels contain common structural motifs in their TM2 segments that are responsible for some of their ion selectivity and conductance properties.

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Language(s): eng - English
 Dates: 1992-07-091992-08-131992-09-04
 Publication Status: Published in print
 Pages: 6
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 Rev. Type: Peer
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Title: Science
  Other : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 257 (5075) Sequence Number: - Start / End Page: 1415 - 1419 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1