Miguel A. Cruz

TL;DR: The crystal structure of the vWF-A1 domain at 2.3-Å resolution is reported, and analysis of the available mutagenesis data suggests that the activator botrocetin binds to the right-hand face of the domain containing helices α5 and α6.

TL;DR: Recombinant vWF-A1 inhibited ristocetin-induced platelet agglutination, but did not compete with vWF multimers for collagen binding, and three recombinant proteins purified as a monomer contained a single disulfide bond provide firm evidence that the major collagen-binding site in vWF resides in the A3 domain.

TL;DR: It is reported that, unlike the I domain of integrin α2β1, vWF-A3 continues to bind collagen after disruption of the motif, and it is concluded that collagen recognition by vWF, a multimeric plasma protein that mediates platelet adhesion to exposed subendothelium at sites of vascular injury, occurs by a mechanism different from that of the integrin β1.

TL;DR: It is document that vWF-A1 domain can bind to GpIb/IX and heparin but not collagen, and that binding to G pIb-IX/IX requires an intact disulfide bond between C509 and C695.

TL;DR: Six mutations located on the front and upper anterior face of the folded vWF-A1 domain, R524S, G561S, H563T, T594S/E596A, Q604R, and S607R, showed reduced activity in all the assays and it is suggested that these residues form part of the GPIb interaction site.