GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins

Curr Opin Struct Biol. 1997 Dec;7(6):786-92. doi: 10.1016/s0959-440x(97)80147-9.

Abstract

Cell biology depends on the interactions of macromolecules, such as protein-DNA, protein-protein or protein-nucleotide interactions. GTP-binding proteins are no exception to the rule. They regulate cellular processes as diverse as protein biosynthesis and intracellular membrane trafficking. Recently, a large number of genes encoding GTP-binding proteins and the proteins that interact with these molecular switches have been cloned and expressed. The 3D structures of some of these have also been elucidated.

Publication types

  • Review

MeSH terms

  • Animals
  • Crystallography, X-Ray
  • GTP Phosphohydrolases / metabolism
  • GTP-Binding Proteins / chemistry*
  • GTP-Binding Proteins / genetics
  • GTP-Binding Proteins / metabolism
  • GTPase-Activating Proteins
  • Guanine Nucleotide Dissociation Inhibitors*
  • Guanine Nucleotide Exchange Factors
  • Guanosine Triphosphate / metabolism
  • Magnetic Resonance Spectroscopy
  • Protein Binding
  • Proteins / chemistry
  • Signal Transduction / physiology
  • ras GTPase-Activating Proteins
  • ras Guanine Nucleotide Exchange Factors
  • ras Proteins / chemistry*
  • ras Proteins / genetics
  • ras Proteins / metabolism
  • rho-Specific Guanine Nucleotide Dissociation Inhibitors

Substances

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