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. 2017 Nov 16;8:1534. doi: 10.1038/s41467-017-01199-8

Fig. 1.

Fig. 1

Fbxo4 directly interacts with Fxr1. a Co-immunoprecipitation of Fbxo4 and Fxr1; arrows indicate Fbxo4 bands. b Endogenous Fbxo4 co-immunoprecipitates with Fxr1. c Ribbon diagram of the Fbxo4:Trf1 heterodimer, PDB:3L82. Fbxo4 is coloured in grey and Trf1 is in purple. d Intermolecular interactions between Fbxo4 and Trf1 derived from the PDB:3L82. e Ribbon diagram of the predicted interaction of Fbxo4 and an Fxr1 homology model. Fbxo4 is coloured in grey and Fxr1 is in purple. f Intermolecular interactions between Fbxo4 and Fxr1. HB is hydrogen bond, HYD is hydrophobic interaction, and ION an ionic bond. g Alignment of a semi-conserved motif in Trf1 and Fxr1. Identical amino acids are highlighted. Residues forming intermolecular bonds in Trf1 are boxed in blue, while residues mutated in this work are boxed in turquoise and magenta. Identity in this region was 30%, while similarity is 65%. h Fbxo4 E379A and E380A mutations disrupt the interaction between Fbxo4 and Fxr1. i Fbxo4 I377M mutation also disrupts the interaction between Fbxo4 and Fxr1. j Fxr1 V178A suppresses, while L189A Fxr1 enhances the interaction between Fbxo4 and Fxr1