[HTML][HTML] The interaction of von Willebrand factor‐A1 domain with collagen: mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in …
LD Morales, C Martin, MA Cruz - Journal of Thrombosis and Haemostasis, 2006 - Elsevier
Background: It is established that the A3 domain in von Willebrand factor (VWF) contains the
major collagen‐binding site. However, there are conflicting reports describing the capacity of
the A1 domain to interact with collagen types I and III. Methods: In this study, we have used
recombinant VWF‐A1 polypeptides, as well as conformation‐specific monoclonal antibodies
(mAb), to analyze the A1–collagen interaction. Results: The A1 domain bound to collagen
with K d∼ 8.0 nm and this binding was blocked by the mAb 6G1, which blocks the …
major collagen‐binding site. However, there are conflicting reports describing the capacity of
the A1 domain to interact with collagen types I and III. Methods: In this study, we have used
recombinant VWF‐A1 polypeptides, as well as conformation‐specific monoclonal antibodies
(mAb), to analyze the A1–collagen interaction. Results: The A1 domain bound to collagen
with K d∼ 8.0 nm and this binding was blocked by the mAb 6G1, which blocks the …
