
DOI . ORG {
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Title[redir]:
GTPase activating proteins: structural and functional insights 18 years after discovery | Cellular and Molecular Life Sciences
Description:
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.
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article, proteins, privacy, cookies, content, molecular, structural, access, information, publish, research, search, gtpase, activating, scheffzek, protein, biology, data, log, journal, life, years, discovery, ahmadian, chapter, discover, author, springer, function, optional, personal, parties, european, policy, find, track, cellular, sciences, cmls, functional, insights, published, november, cite, explore, guanosine, gtp, transport, interaction, gaps,
Topics {✒️}
gnbp-mediated gtp hydrolysis gtpase activating proteins month download article/chapter gα-binding privacy choices/manage cookies transport processes author correspondence function full article pdf european economic area scope submit manuscript computational biology programme developmental biology programme max-planck-institute otto-hahn-strasse 1 conditions privacy policy functional insights 18 years gpcr proteins check access instant access accepting optional cookies gtp discovery review published journal finder publish molecular physiology article cellular life sci structural research information related subjects article log privacy policy personal data direct interaction books a optional cookies manage preferences article cite article scheffzek subscription content similar content data protection eighteen years essential cookies cookies skip structural biology institution subscribe journal publish usage analysis social media
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headline:GTPase activating proteins: structural and functional insights 18 years after discovery
description: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.
datePublished:2005-11-28T00:00:00Z
dateModified:2005-11-28T00:00:00Z
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Signal transduction
cancer
GTPase cycle
arginine finger
switch region
cytoskeleton
nuclear transport
protein targeting
Cell Biology
Biomedicine
general
Life Sciences
Biochemistry
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headline:GTPase activating proteins: structural and functional insights 18 years after discovery
description: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.
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cancer
GTPase cycle
arginine finger
switch region
cytoskeleton
nuclear transport
protein targeting
Cell Biology
Biomedicine
general
Life Sciences
Biochemistry
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