| Title : Molecular cloning of the antagonist-binding subunit of the glycine receptor - Grenningloh_1988_J.Recept.Res_8_183 |
| Author(s) : Grenningloh G , Rienitz A , Schmitt B , Methfessel C , Zensen M , Beyreuther K , Gundelfinger ED , Betz H |
| Ref : J Recept Res , 8 :183 , 1988 |
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Abstract :
The postsynaptic receptor for the inhibitory neurotransmitter glycine is a heterooligomeric membrane protein which, after affinity purification on an antagonist column, contains three polypeptides of 48K, 58K and 93K. Sequencing of cDNA clones of the antagonist-binding 48K subunit revealed a structural organization similar to and significant amino acid homology with nicotinic acetylcholine receptor proteins. Our data suggest the existence of a set of related genes encoding transmembrane channel-forming neurotransmitter receptor polypeptides of excitable membranes. |
| PubMedSearch : Grenningloh_1988_J.Recept.Res_8_183 |
| PubMedID: 2838615 |
Grenningloh G, Rienitz A, Schmitt B, Methfessel C, Zensen M, Beyreuther K, Gundelfinger ED, Betz H (1988)
Molecular cloning of the antagonist-binding subunit of the glycine receptor
J Recept Res
8 :183
Grenningloh G, Rienitz A, Schmitt B, Methfessel C, Zensen M, Beyreuther K, Gundelfinger ED, Betz H (1988)
J Recept Res
8 :183