Cloning and expression of an inwardly rectifying ATP-regulated potassium channel

Nature. 1993 Mar 4;362(6415):31-8. doi: 10.1038/362031a0.

Abstract

A complementary DNA encoding an ATP-regulated potassium channel has been isolated by expression cloning from rat kidney. The predicted 45K protein, which features two potential membrane-spanning helices and a proposed ATP-binding domain, represents a major departure from the basic structural design characteristic of voltage-gated and second messenger-gated ion channels. But the presence of an H5 region, which is likely to form the ion conduction pathway, indicates that the protein may share a common origin with voltage-gated potassium channel proteins.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / pharmacology*
  • Amino Acid Sequence
  • Animals
  • Barium / pharmacology
  • Barium Compounds*
  • Base Sequence
  • Cell Membrane / physiology
  • Cell Membrane / ultrastructure
  • Chlorides*
  • Cloning, Molecular
  • Female
  • Ion Channel Gating
  • Kidney Medulla / physiology*
  • Membrane Potentials / drug effects
  • Models, Structural
  • Molecular Sequence Data
  • Oocytes / drug effects
  • Oocytes / physiology
  • Open Reading Frames
  • Poly A / genetics
  • Potassium Channels / drug effects
  • Potassium Channels / genetics*
  • Potassium Channels / physiology
  • Protein Conformation
  • Protein Structure, Secondary
  • RNA / genetics
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Rats
  • Second Messenger Systems
  • Sequence Homology, Amino Acid
  • Xenopus laevis

Substances

  • Barium Compounds
  • Chlorides
  • Potassium Channels
  • RNA, Messenger
  • barium chloride
  • Poly A
  • Barium
  • RNA
  • Adenosine Triphosphate