Figure 2
From: Rational design of a helical peptide inhibitor targeting c-Myb–KIX interaction
Rational design of Myb32 mutants. (a) Mutation sites (magenta spheres) of Myb32 (blue) mapped onto the c-Myb–KIX complex structure. The figure was drawn using the PyMOL Molecular Graphics System, Version 2.4.0 Schrödinger, LLC. (b) Solvent accessible surface area (SASA) of the c-Myb residues in the c-Myb–KIX complex. (c) Residue-specific helical propensity of Myb32 predicted by AGADIR. The helical propensity of a whole peptide was obtained as an average of these values. (d–h) Helical propensities of the wild type (WT, black) and mutants (red or gray) of Myb32 predicted by AGADIR. For each site, mutations are sorted in the decreasing order of the helical propensity. (i) Helical propensities predicted by AGADIR for the single, double, and triple mutants of Myb32 used in the present study.
