American Society of Hematology

Figure 5.

$Type 2A VWD associated mutations in D1D2 and D’D3. The clinically identified VWD mutations in D1D2 (A) and D’D3 (B) are mapped on the structures by yellow spheres. These mutations either disrupt the local packing of individual domains or interfere with the intermolecular interactions, leading to impaired alignment of 2 D’D3 domains for their dimeric disulfide linkages. Detailed structural analysis of each mutation is provided in supplemental Figure 6. The Y87S, E8del, and Δ437-442 mutation were highlighted in red. (C) The effect of Tyr87 mutations on oligomerization. The D1-D3 variants with the furin cleavage site mutated were analyzed by a Superose 6 gel filtration column with elution curves at pH7.4 with EDTA shown in blue and at pH6 with calcium shown in red. The corresponding fractions were analyzed by SDS-PAGE.$

Type 2A VWD associated mutations in D1D2 and D’D3. The clinically identified VWD mutations in D1D2 (A) and D’D3 (B) are mapped on the structures by yellow spheres. These mutations either disrupt the local packing of individual domains or interfere with the intermolecular interactions, leading to impaired alignment of 2 D’D3 domains for their dimeric disulfide linkages. Detailed structural analysis of each mutation is provided in supplemental Figure 6. The Y87S, E8del, and Δ437-442 mutation were highlighted in red. (C) The effect of Tyr87 mutations on oligomerization. The D1-D3 variants with the furin cleavage site mutated were analyzed by a Superose 6 gel filtration column with elution curves at pH7.4 with EDTA shown in blue and at pH6 with calcium shown in red. The corresponding fractions were analyzed by SDS-PAGE.

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