Fig. 3: Dimer and loop mutations modulate MAX binding affinity. | Nature Communications

Fig. 3: Dimer and loop mutations modulate MAX binding affinity.

From: Mutations to transcription factor MAX allosterically increase DNA selectivity by altering folding and binding pathways

Fig. 3

a Cartoon illustrating double mutant cycles across the TF/DNA interface. b Histograms of Kds for all MAX mutants against each measured E-box; vertical lines denote WT. c Measured ΔΔG relative to WT across all E-boxes (median ± SEM). Red highlights indicate affinity altering mutations (Methods). d Affinity-altering mutations projected on MAX structure (1HLO). Kds (median ± SEM) for all E-box sequences (left), location of residues of interest (red) within MAX structure (1HLO, right) for MAX P51L (e) and N78K (f), with cartoon illustrating impact of mutations on DNA-binding landscape (right). Replicate counts for all Kd measurements are contained in Supplementary Data 1. Source data are provided as a Source Data file.

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