Abstract:
:The primary structure of a novel subunit of the mouse NMDA (N-methyl-D-aspartate) receptor channel, designated epsilon 4, has been revealed by cloning and sequencing the cDNA. The epsilon 4 subunit shares high amino acid sequence identity with the epsilon 1, epsilon 2 and epsilon 3 subunits of the mouse NMDA receptor channel, thus constituting the epsilon subfamily of the glutamate receptor channel. Expression from cloned cDNAs of the epsilon 4 subunit together with the zeta 1 subunit in Xenopus oocytes yields functional NMDA receptor channels. The epsilon 4/zeta 1 heteromeric channel exhibits high apparent affinities for agonists and low sensitivities to competitive antagonists. The epsilon 4 subunit is thus distinct in functional properties from the epsilon 1, epsilon 2 and epsilon 3 subunits, and contributes further diversity of the NMDA receptor channel.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ikeda K,Nagasawa M,Mori H,Araki K,Sakimura K,Watanabe M,Inoue Y,Mishina Mdoi
10.1016/0014-5793(92)81178-okeywords:
subject
Has Abstractpub_date
1992-11-16 00:00:00pages
34-8issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(92)81178-Ojournal_volume
313pub_type
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