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. Author manuscript; available in PMC: 2019 Apr 19.
Published in final edited form as: Cell. 2018 Apr 19;173(3):693–705.e22. doi: 10.1016/j.cell.2018.03.003

Figure 5. Kapβ2 interacts with disordered RGG regions.

Figure 5

Attenuation of glycine resonances in 1H/15N HSQC NMR spectra of 15N-FUS(164–500) (A), RGG1 (B), RGG2-ZnF (C) and ZnF-RGG3 (D) upon addition of 2-fold molar excess of Kapβ2•M9M. E–F) Selected glycine amide resonances of RGG2 (E) and RGG3 (F, left) in 1H-15N HSQC spectra ± 2-fold molar excess Kapβ2•M9M. F) Right, selected glycine amide resonances of RGG3 in 1H-15N TROSY-based cross saturation transfer experiments in the presence of a 1.5-fold molar excess of Kapβ2•M9M with off- or on-resonance saturation. Cross saturation experiment was performed on 2H/15N-FUS(164–500) complexed with unlabeled Kapβ2•M9M in 1:1.5 molar ratio. See also Figure S5, Tables S2 and S3.