The guanine nucleotide-binding switch in three dimensions

Science. 2001 Nov 9;294(5545):1299-304. doi: 10.1126/science.1062023.

Abstract

Guanine nucleotide-binding proteins regulate a variety of processes, including sensual perception, protein synthesis, various transport processes, and cell growth and differentiation. They act as molecular switches and timers that cycle between inactive guanosine diphosphate (GDP)-bound and active guanosine triphosphate (GTP)-bound states. Recent structural studies show that the switch apparatus itself is a conserved fundamental module but that its regulators and effectors are quite diverse in their structures and modes of interaction. Here we will try to define some underlying principles.

Publication types

  • Review

MeSH terms

  • Allosteric Regulation
  • Binding Sites
  • GTP Phosphohydrolases / metabolism
  • GTP-Binding Proteins / chemistry*
  • GTP-Binding Proteins / metabolism*
  • GTPase-Activating Proteins / chemistry
  • GTPase-Activating Proteins / metabolism
  • Guanine Nucleotide Dissociation Inhibitors / chemistry
  • Guanine Nucleotide Dissociation Inhibitors / metabolism
  • Guanine Nucleotide Exchange Factors / chemistry
  • Guanine Nucleotide Exchange Factors / metabolism
  • Guanosine Diphosphate / metabolism
  • Guanosine Triphosphate / metabolism*
  • Hydrolysis
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Tertiary

Substances

  • GTPase-Activating Proteins
  • Guanine Nucleotide Dissociation Inhibitors
  • Guanine Nucleotide Exchange Factors
  • Guanosine Diphosphate
  • Guanosine Triphosphate
  • GTP Phosphohydrolases
  • GTP-Binding Proteins