Fig. 1: Amino acid sequence, structure, and DNA specificity of MAX and Pho4. | Nature Communications

Fig. 1: Amino acid sequence, structure, and DNA specificity of MAX and Pho4.

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

Fig. 1

a Schematic of folding and binding pathway and structural alignment for Pho4 (orange, 1A0A) and MAX (teal, 1HLO). b Domain architectures and sequence alignment for MAX and Pho4 DNA binding domains alongside conservation across bHLH TFs. c Crystallographic contacts between the CACGTG consensus E-box and MAX (teal) and Pho4 (orange). d PWMs for MAX (JASPAR MA0058.3) and Pho4 (JASPAR MA0357.1). e Distribution of binding affinities for all degenerate E-box motif variants25 with most tightly bound sequences annotated (left); median affinity as a function of Hamming distance away from the CACGTG cognate. f Cartoon illustrating differential selectivity. g Classification of MAX mutations in this study. h Microfluidic device and schematic of TFs immobilized on a surface with biotinylated BSA (bBSA), neutravidin (NA), and anti-GFP antibody (left) along with location and identity of MAX mutations studied here (right).

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