Fig. 3: Effects of β2AR peptides and PIP2 binding on βarr1 conformational dynamics probed by 19F NMR. | Nature Communications

Fig. 3: Effects of β2AR peptides and PIP2 binding on βarr1 conformational dynamics probed by 19F NMR.

From: Distinct activation mechanisms of β-arrestin-1 revealed by 19F NMR spectroscopy

Fig. 3

a Sequence and phosphorylation sites of the β2AR-GRK2pp, β2AR-GRK6pp compared with V2Rpp. The numbering of the eight phosphorylation sites in V2Rpp is indicated. b 19F NMR spectra of the gate loop H295C site in different states. c 19F NMR spectra showing the effects of β2AR-GRK2pp, -GRK6pp and PIP2 binding on the conformational dynamics at the central crest region. d 19F NMR spectra of the CT D390C site showing the effects of V2Rpp peptide variants, β2AR-GRK2pp, -GRK6pp, and PIP2 binding. V2Rd678pp, V2Rd5pp and V2Rd12pp denotes that the last three, the fifth and the first two phosphorylation sites are unphosphorylated, respectively. The spectra of the V2Rpp-bound state are shown in magenta dashed lines in b–d for comparison. e A schematic illustration showing the binding of the 5, 6, and 7th phosphates of V2Rpp to critical structural regions of the βarr1 N-domain.

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