Аннотация
To characterize the mechanism by which heterotrimeric G-proteins interpret
the signals coming from various neurotransmitters of diverse efficacies
(agonists and partial agonists) acting on alpha(2A)-adrenergic receptors,
we used a fluorescent resonance energy transfer-based approach to
study the effects of these partial agonists on the activation process
of both the alpha(2A)-adrenergic receptor and its cognate G(i)-protein.
We show that ligands of different efficacies switch the receptor
into distinct conformational states, which in turn set the speed
and extent of the G(i)-protein signaling. Thus, in cells the efficacy
by which a receptor responds to diverse ligands is caused by the
ability of the G-protein to differentiate between distinct receptor
conformations. The data provide a new key characteristic underlying
the mechanism of partial agonism at G-protein-coupled receptors.
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