Abstract
While the structural mechanism of G protein-coupled receptor (GPCR) activation is well studied, there is sparse information concerning the functional role of the intrinsically disordered intracellular loops of the receptor in said mechanism. We show that the third intracellular loop (ICL3) of the beta 2 adrenergic receptor (β2AR) autoregulates receptor activation and G protein-mediated signaling. Using a combination of time resolved fluorescence spectroscopy and molecular dynamics simulations, we find that ICL3 is in an equilibrium between an ensemble of closed and open conformational states.
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