Supplementary Figure 1: 2D 1H-15N HSQC NMR spectrum of β2AR NMR titrations. | Nature Structural & Molecular Biology

Supplementary Figure 1: 2D 1H-15N HSQC NMR spectrum of β2AR NMR titrations.

From: A molecular code for endosomal recycling of phosphorylated cargos by the SNX27–retromer complex

Supplementary Figure 1

(related to Fig. 4)

(a) Overlays of the 2D 1H-15N HSQC spectra of 15N-13C-labeled SNX27 PDZ domain in its free form (blue) and titrated with between 0.5 to 4 molar equivalents of β2AR-pS-6 peptide. Resonances showing significant broadening and changes in chemical shift on β2AR-pS-6 binding are labelled with the residue number. Residues which chemical shift variation superior to Δδ=0.4 ppm are labelled on the histogram in the lower box. (b) Overlays of the 2D 1H-15N HSQC spectra of 15N-13C-labeled SNX27PDZ in its free form (black) and in the presence of 0.5 to 4 molar equivalents of β2AR or β2AR-pS-2. Resonances showing significant broadening and changes in chemical shift on VPS26A binding are labelled with the residue number.

Back to article page