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. Author manuscript; available in PMC: 2023 Feb 27.
Published in final edited form as: Biochem Biophys Res Commun. 2021 Jun 22;567:208–214. doi: 10.1016/j.bbrc.2021.06.047

Fig. 3.

Fig. 3.

RepID WD40 domain consists of two β-propeller folds linked by a loop. (A) Molecular modeling of the RepID WD40 domain was performed using Swiss-Model (http://swissmodel.expasy.org). The positions of N-terminal, C-terminal regions with two β-propeller folds (BPA and BPB) involving 9 blades composed of a three- or four-stranded antiparallel β-sheet are indicated (left and middle panel). The loop region is indicated with amino acid positions (right panel). β-helix and β-sheets are represented as purple and green, respectively. (B) Amino acid positions of each β-sheet in the 9 blades located in 9 exon-containing WD40 domains. Predicted loop and α-helix is indicated in red. (C) RaptorX server-based prediction (http://raptorx.uchicago.edu/StructurePropertyPred/predict/). Bar graph represents percentage of 8-state secondary structures (H, α-helix; G, 3helix; I, 5-helix; E, extended strand in β-ladder; B, isolated β-bridge; T, hydrogen bonded turn; S, bend; L, loop) in each exon. Numbers in exon 3 (red) represents fold change compared to average percentage of other mutants.