β₂-Adrenergic Receptor Conformational Response to Fusion Protein in the Third Intracellular Loop.

ABSTRACT: Fluorine-19 nuclear magnetic resonance (NMR) was used to study conformational equilibria at the intracellular tips of helices VI and VII in a variant β₂-adrenergic receptor (β₂AR) containing T4-lysozyme fused into the third intracellular loop (β₂AR-T4L), a G protein-coupled receptor (GPCR) modification widely used in crystal structure determination. G-protein signaling at helix VI showed nearly complete population of an active-like state for all ligand efficacies in the absence of an intracellular protein. For arrestin signaling at helix VII, a native-like equilibrium was observed, except for complexes with ligands devoid of a hydrophobic moiety at the ethanolamine end. These data confirm that response of G-protein and arrestin signaling to ligand efficacy

SUBMITTER: Eddy MT 

PROVIDER: S-EPMC5144828 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature