Fig. 4: Negative constraints on DIP-α, blue Dprs 6/10, and DIP-γ that inhibit purple/blue inter-subgroup binding.
From: DIP/Dpr interactions and the evolutionary design of specificity in protein families
a Negative constraints on DIP-α. Alignment of interfacial residues of DIP-α and DIP-γ followed by structural details used to explain negative constraint. The average KD and the experimental error for wild-type DIP-γ/Dpr11 interaction based on five independent experimental measurements is given on the left of the alignment. Experimental KDs and ΔΔGs relative to wild type DIP-α/Dpr11 are shown below each insert. All symbols as in Fig. 3. b Negative constraints on Dprs 6/10. Alignment of interfacial residues of Dpr6 and Dpr10 with Dpr11. All other details as in a. c Negative constraints on DIP-γ. Alignment of interfacial residues of DIP-α and DIP-γ. All other details as in a. The supporting SPR data for the mutants presented in a–c can be found in Supplementary Fig. 3A–C. For each KD, the number in parenthesis represents the fitting error in the last significant figure, in μM for a single experiment with an expected experimental error up to 15%. Source data are provided as a Source Data file.
