Structural aspects of heterotrimeric G-protein signaling.
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.
Bohm
A
A
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA.
Gaudet
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R
Sigler
P B
PB
D000818:Animals; D005136:Eye Proteins / Q000737:chemistry / Q000378:metabolism; D020555:GTP-Binding Protein Regulators; D019204:GTP-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D046911:Macromolecular Substances; D008954:Models, Biological; D008961:Models, Structural; D016297:Mutagenesis, Site-Directed; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D011956:Receptors, Cell Surface / Q000502:physiology; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction
D005136:Eye Proteins; D020555:GTP-Binding Protein Regulators; D046911:Macromolecular Substances; D010750:Phosphoproteins; D011956:Receptors, Cell Surface; D011994:Recombinant Proteins; C065631:phosducin; D019204:GTP-Binding Proteins