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PMID: 8524912 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Determination of NMDA NR1 subunit copy number in recombinant NMDA receptors.

Proceedings. Biological sciences ·Vol. 262 ·No. 1364 ·1995-11-22 ·Pages 205-13

Béhé P, Stern P, Wyllie DJ, Nassar M, Schoepfer R, Colquhoun D

Abstract

Co-expression of wild-type and mutated NMDA NR1 (N598R) subunits in Xenopus oocytes has been used to determine the stoichiometry of the NMDA receptor-channel. When expressed together, wild-type NR2A and mutant NR1 (N598R) subunits produced channels with a main conductance of 2.6 pS and a sublevel of 1.2 pS. These conductances were clearly different from those obtained from wild-type NR1 and wild-type NR2A channels which gave characteristic 50 pS events with a 40 pS sublevel. When wild-type and mutant NR1 subunits were co-expressed together with NR2A subunits a different channel type with a main conductance of 15.2 pS and a sublevel of 11.4 pS was obtained, as well as the 'all wild-type' and 'all mutant' channels described above. These results indicate that there are likely to be two copies of the NR1 subunit in each NMDA receptor complex.

MeSH Terms
Animals Glutamic Acid/metabolism Mutation Protein Structure, Secondary Receptors, N-Methyl-D-Aspartate/genetics,metabolism Recombinant Proteins/genetics,metabolism Xenopus
Chemicals
Receptors, N-Methyl-D-Aspartate Recombinant Proteins Glutamic Acid
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Béhé P
Department of Pharmacology, University College London, U.K.
Stern P
Wyllie D J
Nassar M
Schoepfer R
Colquhoun D
Article Info
Journal
Proceedings. Biological sciences
Abbr.
Proc Biol Sci
ISSN
0962-8452
Published
1995-11-22
Pages
205-13
Language
English
Region
England
NLM ID
101245157
Subset
IM
Grants
Wellcome Trust · United Kingdom
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