Figure 1. Structure of VWF and ADAMTS13. VWF multimers may contain ≥40 ∼250 kDa subunits linked together by disulfide bonds between C-terminal cystine-knot (CK) domains and N-terminal D3 domains. The VWF subunit is composed mostly of repeated A, C, and D domains and has binding sites for many proteins, including factor VIII, platelet GPIb, and collagens (Col) 1, 3, and 6. The A2 domain has a globular structure in native VWF, but unfolds in response to fluid shear stress to expose a Tyr-Met bond (red triangle) that is cleaved by ADAMTS13. ADAMTS13 is a multidomain protein with metalloprotease (M), disintegrin-like (D), thrombospondin type 1, Cys-rich, spacer, 7 more thrombospondin type 1 repeats, and 2 CUB domains. A molecular model of the proximal domains shows sites (shaded red) that interact with the extended sequence of the A2 domain.
Figure 1.

Structure of VWF and ADAMTS13. VWF multimers may contain ≥40 ∼250 kDa subunits linked together by disulfide bonds between C-terminal cystine-knot (CK) domains and N-terminal D3 domains. The VWF subunit is composed mostly of repeated A, C, and D domains and has binding sites for many proteins, including factor VIII, platelet GPIb, and collagens (Col) 1, 3, and 6. The A2 domain has a globular structure in native VWF, but unfolds in response to fluid shear stress to expose a Tyr-Met bond (red triangle) that is cleaved by ADAMTS13. ADAMTS13 is a multidomain protein with metalloprotease (M), disintegrin-like (D), thrombospondin type 1, Cys-rich, spacer, 7 more thrombospondin type 1 repeats, and 2 CUB domains. A molecular model of the proximal domains shows sites (shaded red) that interact with the extended sequence of the A2 domain.

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