Abstract
Recently, structures of heterotrimeric G-protein subunits have been determined in isolation, in conjunction with each other, and in complex with their regulators. Along with biochemical information, these structures suggest how G-protein subunits are oriented relative to the membrane surface and relative to seven-transmembrane helix receptors. They also suggest mechanisms for receptor-catalyzed nucleotide exchange.
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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Animals
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Eye Proteins / chemistry
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Eye Proteins / metabolism
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GTP-Binding Protein Regulators
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GTP-Binding Proteins / chemistry*
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GTP-Binding Proteins / metabolism*
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Macromolecular Substances
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Models, Biological
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Models, Structural
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Mutagenesis, Site-Directed
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Phosphoproteins / chemistry
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Phosphoproteins / metabolism
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Protein Structure, Secondary*
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Receptors, Cell Surface / physiology
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Signal Transduction*
Substances
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Eye Proteins
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GTP-Binding Protein Regulators
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Macromolecular Substances
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Phosphoproteins
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Receptors, Cell Surface
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Recombinant Proteins
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phosducin
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GTP-Binding Proteins