The GTPase superfamily: conserved structure and molecular mechanism

Nature. 1991 Jan 10;349(6305):117-27. doi: 10.1038/349117a0.

Abstract

GTPases are conserved molecular switches, built according to a common structural design. Rapidly accruing knowledge of individual GTPases--crystal structures, biochemical properties, or results of molecular genetic experiments--support and generate hypotheses relating structure to function in other members of the diverse family of GTPases.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • GTP Phosphohydrolase-Linked Elongation Factors / physiology*
  • GTP Phosphohydrolase-Linked Elongation Factors / ultrastructure
  • GTP-Binding Proteins / metabolism
  • Guanosine Diphosphate / metabolism
  • Guanosine Triphosphate / metabolism
  • Humans
  • Molecular Sequence Data
  • Peptide Elongation Factors / metabolism
  • Peptide Initiation Factors / metabolism
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Proto-Oncogene Proteins p21(ras) / metabolism
  • Signal Transduction

Substances

  • Peptide Elongation Factors
  • Peptide Initiation Factors
  • Guanosine Diphosphate
  • Guanosine Triphosphate
  • GTP Phosphohydrolase-Linked Elongation Factors
  • GTP-Binding Proteins
  • HRAS protein, human
  • Proto-Oncogene Proteins p21(ras)