Fig. 1: Structural mechanism for the interaction of Taf14_ET with Taf2_CT.

a Architecture of Taf14_FL. b Superimposed ¹H¹⁵,N HSQC spectra of Taf14_ET recorded in the presence of increasing amounts of the Taf2_CT peptide. The spectra are color coded according to the protein:peptide molar ratio. c MST binding curve for the FAM-Taf2_CT interaction with Taf14_ET. The K_d value represents average (shown as red diamonds) of three independent measurements (open circles), and error bars represent the standard deviation from average. n = 3 d Electrostatic surface potential of the crystal structure of the Taf14_ET:Taf2_CT complex, with blue and red colors representing positive and negative charges, respectively. The Taf2_CT peptide is shown as a purple ribbon. e Ribbon diagram of the Taf14_ET:Taf2_CT complex structure in the same orientation as in (d). Taf14_ET domain is colored wheat and Taf2_CT peptide is purple. Residues involved in the interaction between Taf2_CT and Taf14_ET are labeled. Dashed lines represent hydrogen bonds. f Rotated view of the ribbon structure shown in (e). Schematic of the Taf14_ET-Taf2_CT complex is shown above the structure. g Superimposed ¹H¹⁵,N HSQC spectra of Taf14_FL recorded in the presence of increasing amounts of the Taf2_CT peptide. The spectra are color coded according to the protein:peptide molar ratio. h MST binding curves for the FAM-Taf2_CT interaction with Taf14_FL. The K_d value represents average of three independent measurements, and error represents the standard deviation. n = 3.