The strychnine-binding subunit of the glycine receptor shows homology with nicotinic acetylcholine receptors

Nature. 1987 Jul 16-22;328(6127):215-20. doi: 10.1038/328215a0.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cloning, Molecular
  • DNA / genetics
  • Membrane Proteins / genetics*
  • Multigene Family
  • Protein Binding
  • Protein Conformation
  • Rats
  • Receptors, Glycine
  • Receptors, Neurotransmitter / genetics*
  • Receptors, Nicotinic / genetics*
  • Sequence Homology, Nucleic Acid
  • Strychnine / metabolism*
  • Tissue Distribution

Substances

  • Membrane Proteins
  • Receptors, Glycine
  • Receptors, Neurotransmitter
  • Receptors, Nicotinic
  • DNA
  • Strychnine

Associated data

  • GENBANK/Y00276