Abstract.
The conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (Pi) 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.
Similar content being viewed by others
Author information
Authors and Affiliations
Corresponding author
Additional information
Received 25 March 2005; received after revision 31 August 2005; accepted 6 September 2005
Rights and permissions
About this article
Cite this article
Scheffzek, K., Ahmadian, M.R. GTPase activating proteins: structural and functional insights 18 years after discovery. Cell. Mol. Life Sci. 62, 3014–3038 (2005). https://doi.org/10.1007/s00018-005-5136-x
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00018-005-5136-x