The strychnine-binding subunit of the glycine receptor shows homology with nicotinic acetylcholine receptors.
We have cloned and sequenced cDNAs of the strychnine-binding subunit of the rat glycine receptor, a neurotransmitter-gated chloride channel protein of the CNS. The deduced polypeptide shows significant structural and amino-acid sequence homology with nicotinic acetylcholine receptor proteins, indicating that there is a family of genes encoding neurotransmitter-gated ion channels.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics*; D005810:Multigene Family; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter / Q000235:genetics*; D011978:Receptors, Nicotinic / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013331:Strychnine / Q000378:metabolism*; D014018:Tissue Distribution
D008565:Membrane Proteins; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter; D011978:Receptors, Nicotinic; D004247:DNA; D013331:Strychnine