Receptor-G protein coupling is established by a potential conformational switch in the beta gamma complex.
Receptor-G protein interaction is characterized by cycles of association and dissociation. We present evidence which indicates that during receptor-G protein interaction, the C-terminal tail of the G protein gamma subunit, which is masked in the beta gamma complex, is exposed and establishes high-affinity contact with the receptor. This potential conformational switch provides a mechanism to regulate receptor-G protein coupling. This switch may also be significant for the role of the beta gamma complex in regulation of effector function.
Kisselev
O
O
Department of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Pronin
A
A
Ermolaeva
M
M
Gautam
N
N
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D002460:Cell Line; D003370:Coturnix; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D015151:Immunoblotting; D007700:Kinetics; D046911:Macromolecular Substances; D008961:Models, Structural; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000276:immunology; D011485:Protein Binding; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012243:Rhodopsin / Q000378:metabolism; D015293:Transducin / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*; D014162:Transfection
D000906:Antibodies; D046911:Macromolecular Substances; D010455:Peptides; D011956:Receptors, Cell Surface; D011994:Recombinant Proteins; D012243:Rhodopsin; D019204:GTP-Binding Proteins; D015293:Transducin