Primary structure and functional expression from complementary DNA of the rod photoreceptor cyclic GMP-gated channel

Nature. 1989 Dec 14;342(6251):762-6. doi: 10.1038/342762a0.

Abstract

The complete amino-acid sequence of the cyclic GMP-gated channel from bovine retinal rod photoreceptors, deduced by cloning and sequencing its complementary DNA, shows that the protein contains several putative transmembrane segments, followed by a region that is similar to the cyclic GMP-binding domains of cyclic GMP-dependent protein kinase. Expression of the complementary DNA produces cyclic GMP-gated channel activity in Xenopus oocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Cloning, Molecular
  • Cyclic GMP / physiology*
  • Cyclic Nucleotide-Gated Cation Channels
  • DNA / genetics
  • Eye Proteins / genetics*
  • In Vitro Techniques
  • Ion Channel Gating
  • Ion Channels / physiology*
  • Membrane Proteins / genetics
  • Molecular Sequence Data
  • Protein Conformation
  • RNA, Messenger / genetics
  • Rod Cell Outer Segment
  • Solubility
  • Xenopus laevis

Substances

  • Cyclic Nucleotide-Gated Cation Channels
  • Eye Proteins
  • Ion Channels
  • Membrane Proteins
  • RNA, Messenger
  • DNA
  • Cyclic GMP