Disease Mutation Study Identifies Critical Residues for Phosphatidylserine Flippase ATP11A

Figure 6

Models of ATP11A mutants. (a) A homology model of ATP11A was constructed based on sequence alignment with other P-type ATPases and available structural data. The transmembrane helices, loop, and sheet are blue, pink, and purple, respectively. (b–h) Target amino acids are shown in yellow, amino acids linked to the target amino acid are shown in green, and hydrogen bonds are shown in red. (b–d) I80 residue is linked to Y76, V83, and Q84, and V80 residue has the same connection. However, P80 residue is only linked to Q84. (e, f) Y300 residue is linked to F296, L304, and nearby I359 positioned on the M3-M4 loop. Nevertheless, F300 residue cannot be connected to I359. (g, h) D913 residue, located at the M5-M6 loop, is linked to Y916 and L917. While the direction of K913 residue changed, and one more T914 was connected.

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