Figure 1: Hydrophobic network of KIX regulating c-Myb recognition.
From: Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein
(Left) Structure of the complex between KIX (red) and c-Myb (blue), shown in cartoon (pdb: 1SB0). The key residues I26, L43 and I72 of KIX, previously identified as critical for ligand binding29,30, are highlighted in balls and sticks. (Right) Pseudo-first order kinetics for the binding of c-Myb to four variants of KIX, i.e. the wild type and three variants I26V, L43A and I72V. Rate constants were obtained by stopped-flow fluorimetry at a fixed concentration of KIX (typically ranging from 3 to 8 μM), mixed with increasing concentrations of c-Myb. All experiments were performed at 10 °C and the buffer used was 50 mM sodium phosphate, 150 mM KCl, 1 mM DTT, pH 7.2.
