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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Neyton, J. Ascher, P. Kupper, J. |
| Description | Author Affiliation: Kupper J ( Laboratoire de Neurobiologie, Centre National de la Recherche Scientifique Unité de Recherche Associée 1857, Ecole Normale Supéricure, Paris, France.); |
| Abstract | Mg2+ ions block N-methyl-D-aspartate (NMDA) channels by entering the pore from either the extracellular or the cytoplasmic side of the membrane in a voltage-dependent manner. We have used these two different block phenomena to probe the structure of the subunits forming NMDA channels. We have made several amino acid substitutions downstream of the Q/R/N site in the TMII region of both NR1 and NR2A subunits. Mutant NR1 subunits were coexpressed with wild-type NR2A subunits and vice versa in Xenopus oocytes. We found that individually mutating the first two amino acid residues downstream to the Q/R/N site affects mostly the block by external Mg2+. Mutations of residues five to seven positions downstream of the Q/R/N site do not influence the external Mg2+ block, but clearly influence the block by internal Mg2+. These data add support to the hypothesis that there are two separate binding sites for external and internal Mg2+ block. They also indicate that the C-terminal end of TMII contributes to the inner vestibule of the pore of NMDA channels and thus provide additional evidence that TMII forms a loop that reemerges toward the cytoplasmic side of the membrane. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 16 |
| Volume Number | 93 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1996-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Ion Channel Gating Drug Effects Ion Channels Physiology Magnesium Pharmacology Receptors, N-Methyl-D-Aspartate Chemistry Amino Acid Sequence Animals Membrane Potentials Molecular Sequence Data Oocytes Patch-Clamp Techniques Recombinant Proteins Structure-Activity Relationship Xenopus Laevis Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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