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. 2017 Apr 20;56(18):2379–2384. doi: 10.1021/acs.biochem.7b00179

Figure 3.

Figure 3

Helix-flanking prolines modulate residual structure in p53 and MLL. Change in per residue fractional helicity estimates upon PtoA mutation for (A) p53 P27A and (B) MLL P9/21A. WT residues that become helical upon binding are underlined. Conserved helix-flanking prolines are highlighted. p53 NMR helicity data are from ref (3). Individual fractional helicity plots for MLL WT and P9/21A are shown in Figure S2B. Estimates from NMR and CD gave similar changes in overall MLL helicity (Table 1). Note that the mean helicity within the region that becomes helical upon binding was increased by 2.5-fold in p53 P27A and 1.4-fold in MLL P9/21A, compared to that of the WT. Helix-flanking prolines are shown as cyan spheres in the structures of (A) p53:MDM2 (PDB entry 1YCR) and (B) MLL:KIX (PDB entry 2LXS). Cyan circles represent helix-flanking prolines that are not present in the structure.