Molecular cloning of the antagonist-binding subunit of the glycine receptor.
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.
Grenningloh
G
G
ZMBH, Universität Heidelberg, FRG.
Rienitz
A
A
Schmitt
B
B
Methfessel
C
C
Zensen
M
M
Beyreuther
K
K
Gundelfinger
E D
ED
Betz
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D004331:Drosophila melanogaster; D005796:Genes; D051381:Rats; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter / Q000235:genetics* / Q000378:metabolism; D011978:Receptors, Nicotinic / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D013331:Strychnine / Q000378:metabolism; D014981:Xenopus
D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter; D011978:Receptors, Nicotinic; D004247:DNA; D013331:Strychnine