1H, 13C, and 15N backbone resonance assignments of the A2 domain of human von Willebrand factor.

The A2 domain of von Willebrand factor (vWF A2) acts as a mechanosensor, unfolding under shear stress to enable cleavage by ADAMTS13. Dysfunction of this process causes von Willebrand disease (VWD) and thrombotic thrombocytopenic purpura (TTP). Although we previously reported the NMR assignments for mouse vWF A2, the human ortholog shares only 79% sequence identity (38 amino acid differences). Given that VWD and TTP are human pathologies, structural characterization of the human protein is essential. Here, we present the backbone 1H, 13C, and 15N resonance assignments of human vWF A2. Secondary structure propensity (SSP) analysis confirms that the solution structure retains the canonical Rossmann fold. Comparison with the mouse ortholog reveals distinct local differences in secondary structure propensities, particularly at the boundaries of α-helices and β-strands. These local variations, arising from sequence divergence, may influence the stability and unfolding dynamics relevant to human disease mechanisms.