Structural aspects of heterotrimeric G-protein signaling

Curr Opin Biotechnol. 1997 Aug;8(4):480-7. doi: 10.1016/s0958-1669(97)80072-9.

Abstract

Recently, structures of heterotrimeric G-protein subunits have been determined in isolation, in conjunction with each other, and in complex with their regulators. Along with biochemical information, these structures suggest how G-protein subunits are oriented relative to the membrane surface and relative to seven-transmembrane helix receptors. They also suggest mechanisms for receptor-catalyzed nucleotide exchange.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Eye Proteins / chemistry
  • Eye Proteins / metabolism
  • GTP-Binding Protein Regulators
  • GTP-Binding Proteins / chemistry*
  • GTP-Binding Proteins / metabolism*
  • Macromolecular Substances
  • Models, Biological
  • Models, Structural
  • Mutagenesis, Site-Directed
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism
  • Protein Structure, Secondary*
  • Receptors, Cell Surface / physiology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Signal Transduction*

Substances

  • Eye Proteins
  • GTP-Binding Protein Regulators
  • Macromolecular Substances
  • Phosphoproteins
  • Receptors, Cell Surface
  • Recombinant Proteins
  • phosducin
  • GTP-Binding Proteins