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Abstract Heterotrimeric G proteins, activated by G-protein-coupled receptors (GPCRs), are central mediators of cellular signaling. Activation requires GDP release from the Gα subunit, a step attributed largely to the C-terminal α5 helix, the primary GPCR-interacting region. Contributions from other Gα regions have remained unclear. Here we show that the N-terminal helix (αN) of Gαs promotes GDP release through a rotational conformational change.
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