GTPase activating proteins: structural and functional insights 18 years after discovery

Cell Mol Life Sci. 2005 Dec;62(24):3014-38. doi: 10.1007/s00018-005-5136-x.

Abstract

The conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (P(i)) by guanine nucleotide binding proteins (GNBPs) is a fundamental process in living cells and represents an important timer in intracellular signalling and transport processes. While the rate of GNBP-mediated GTP hydrolysis is intrinsically slow, direct interaction with GTPase activating proteins (GAPs) accelerates the reaction by up to five orders of magnitude in vitro. Eighteen years after the discovery of the first GAP, biochemical and structural research has been accumulating evidence that GAPs employ a much wider spectrum of chemical mechanisms than had originally been assumed, in order to regulate the chemical players on the catalytic protein-protein interaction stage.

Publication types

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

MeSH terms

  • Animals
  • GTPase-Activating Proteins / chemistry*
  • GTPase-Activating Proteins / physiology*
  • Humans
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Tertiary
  • Substrate Specificity

Substances

  • GTPase-Activating Proteins