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Updated: Aug 18, 2026

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
Published on: July 28, 2014
Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein
D G Lambright1, J P Noel, H E Hamm
1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510.
Abstract:
The 1.8 A crystal structure of transducin alpha.GDP, when compared to that of the activated complex with GTP-gamma S, reveals the nature of the conformational changes that occur on activation of a heterotrimeric G-protein alpha-subunit. Structural changes initiated by direct contacts with the terminal phosphate of GTP propagate to regions that have been implicated in effector activation. The changes are distinct from those observed in other members of the GTPase superfamily.
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