Figure 2
Figure 2. Structural analysis. Positions of aHUS-associated mutations found in this study (D254 and K325), in relation to the MIDAS site (in ball and stick representation) and previously found mutations of F261 and K2988 on the VWF-A domain of factor B. The aHUS-associated mutations described by Goicoechea de Jorge et al have been originally named according to the protein numbering with the leader peptide.8 For clarity in this work, the number of both previously described residues is given according to the protein structure: F286 is F261 here and K323 is K298 here.

Structural analysis. Positions of aHUS-associated mutations found in this study (D254 and K325), in relation to the MIDAS site (in ball and stick representation) and previously found mutations of F261 and K298 on the VWF-A domain of factor B. The aHUS-associated mutations described by Goicoechea de Jorge et al have been originally named according to the protein numbering with the leader peptide. For clarity in this work, the number of both previously described residues is given according to the protein structure: F286 is F261 here and K323 is K298 here.

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