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. 2016 Jun 2;113(24):E3403–E3412. doi: 10.1073/pnas.1603269113

Fig. S3.

Fig. S3.

Characterization of pMAVS and pTRIF peptides. (A) MALDI-TOF MS analysis of phosphorylated human MAVS (residues 433–450, M449W) peptide. The M449W mutation was introduced in this peptide for quantification purposes. (B) SPR binding studies of phosphorylated and unphosphorylated MAVS (residues 433–450, M449W) peptide with IRF-3. (C) Binding affinity between pMAVS (residues 433–450, M449W) peptide and IRF-3. (D) SPR binding studies of pMAVS (residues 400–491) peptide with IRF-3. (E) Binding affinity between pMAVS (residues 400–491) peptide and IRF-3. (F) MALDI-TOF MS analysis of phosphorylated human TRIF (residues 199–219, L218W) peptide. (G) SPR binding studies of phosphorylated and unphosphorylated TRIF (residues 199–219, L218W) peptide with IRF-3. (H) Binding affinity between pTRIF (residues 199–219, L218W) peptide and IRF-3.