FIGURE 2

FIGURE 2

Predicted WARP structures, protein interactions and conserved domains. (A) Predicted secondary structures of wild-type and mutant protein sequences flanking the mutation. Secondary structural features are annotated as follows: pink cylinder, α-helix; yellow arrow, β-sheet; black line, coil; Conf, confidence; Pred, predicted; H in Pred line, helix; C in Pred line, coil; E in Pred line, sheet; AA, amino acid; red arrow, mutant amino acid. Local (B) and global (C) views of the predicted tertiary structures of wild-type (green) and mutant (blue) proteins. Structural superposition analyses demonstrating the change in protein structure brought about by the mutation are also displayed. (D) Protein-to-protein interactions of WARP with the FGF pathway. Predictions using the web-based program, String, indicated that WARP may functionally interact with four proteins of FGF pathway: FGF23, SPP1, CDH2, and SDC2. (E) Domains of WARP conserved in humans and zebrafish. Humans and zebrafish have the same WARP conserved domains: a von Willebrand factor A-domain, the first fibronectin type III repeat, and the second fibronectin type III repeat.