Fig. 3

The 3D structure for CEP57L: a Phyre2 was used to create the model, which 95 % of the 460 residues were modeled at >90 % confidence using 1CII as a template, b Residues 1 to 18 (yellow) are zoomed in and is also the remaining structure—the bottom left disordered region in a—from the exon deletion and are surrounded by an α-helical-dominant protein, and c the result from the absence of the surrounding helices as they form a higher-ordered-α-helical structure predicted by PEP-FOLD in which intermolecular interactions may have contributed to a more disordered behavior