Figure 7 of Li, Mol Vis 2014; 20:1-14.

Figure 7. AIPL1 protein domains, structure, and the effect of the R258P mutation. A: AIPL1 domains including the FKBP-type peptidyl-prolyl cis-trans isomerase (FKBP_C, yellow) domain, The tetratricopeptide repeat (TPR, green) domain, with three individual repeat domains (TPR1, TPR 2, and TPR 3, smaller green rectangles above the ruler), individual TPR motifs (blue tics above the TPR domain), and binding surfaces (maroon tics above the TPR domain). B: Modeled structures of theR258 (left) and P258 (right) 117 amino acid AIPL1 TPR domains with alpha helices shown in pink, turns shown in blue, and random coils shown in white. The R258 and P258 residues are shown in ball-and-stick form in red. The insets at the bottom left corner of each panel show the R258 residue residing near the end of the alpha helix of the second TPR repeat domain, and the P258 residue disrupting the helical structure so that the helix is shortened and the P258 and adjacent residues assume a turn structure.