G proteins, effectors and GAPs: structure and mechanism

Curr Opin Struct Biol. 1997 Dec;7(6):849-56. doi: 10.1016/s0959-440x(97)80157-1.

Abstract

G proteins from a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effectors. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.

Publication types

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

MeSH terms

  • Binding Sites
  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / metabolism
  • GTP-Binding Proteins / chemistry*
  • GTP-Binding Proteins / metabolism
  • GTPase-Activating Proteins
  • Guanosine Triphosphate / chemistry
  • Guanosine Triphosphate / metabolism
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / metabolism
  • Proto-Oncogene Proteins p21(ras) / chemistry
  • Proto-Oncogene Proteins p21(ras) / metabolism
  • ras GTPase-Activating Proteins
  • ras Proteins / chemistry*
  • ras Proteins / metabolism

Substances

  • GTPase-Activating Proteins
  • Proteins
  • ras GTPase-Activating Proteins
  • Guanosine Triphosphate
  • GTP Phosphohydrolases
  • GTP-Binding Proteins
  • Proto-Oncogene Proteins p21(ras)
  • ras Proteins