Abstract
Guanine nucleotide-binding proteins regulate a variety of processes, including sensual perception, protein synthesis, various transport processes, and cell growth and differentiation. They act as molecular switches and timers that cycle between inactive guanosine diphosphate (GDP)-bound and active guanosine triphosphate (GTP)-bound states. Recent structural studies show that the switch apparatus itself is a conserved fundamental module but that its regulators and effectors are quite diverse in their structures and modes of interaction. Here we will try to define some underlying principles.
MeSH terms
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Allosteric Regulation
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Binding Sites
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GTP Phosphohydrolases / metabolism
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GTP-Binding Proteins / chemistry*
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GTP-Binding Proteins / metabolism*
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GTPase-Activating Proteins / chemistry
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GTPase-Activating Proteins / metabolism
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Guanine Nucleotide Dissociation Inhibitors / chemistry
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Guanine Nucleotide Dissociation Inhibitors / metabolism
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Guanine Nucleotide Exchange Factors / chemistry
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Guanine Nucleotide Exchange Factors / metabolism
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Guanosine Diphosphate / metabolism
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Guanosine Triphosphate / metabolism*
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Hydrolysis
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Models, Molecular
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Protein Conformation
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Protein Structure, Tertiary
Substances
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GTPase-Activating Proteins
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Guanine Nucleotide Dissociation Inhibitors
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Guanine Nucleotide Exchange Factors
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Guanosine Diphosphate
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Guanosine Triphosphate
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GTP Phosphohydrolases
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GTP-Binding Proteins