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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Binding Sites
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GTP Phosphohydrolases / chemistry
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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
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Guanosine Triphosphate / chemistry
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Guanosine Triphosphate / metabolism
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Models, Molecular
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Protein Binding
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Protein Conformation
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Proteins / chemistry*
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Proteins / metabolism
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Proto-Oncogene Proteins p21(ras) / chemistry
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Proto-Oncogene Proteins p21(ras) / metabolism
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ras GTPase-Activating Proteins
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ras Proteins / chemistry*
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ras Proteins / metabolism
Substances
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GTPase-Activating Proteins
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Proteins
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ras GTPase-Activating Proteins
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Guanosine Triphosphate
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GTP Phosphohydrolases
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GTP-Binding Proteins
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Proto-Oncogene Proteins p21(ras)
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ras Proteins