ADAMTS13 R1206K Variant Exhibits an Open Conformation and Enhanced Proteolytic Activity toward von Willebrand factor
These results demonstrate that ADAMTS13 R1206K variant has an enhanced enzymatic activity, resulting from the disruption of autoinhibition that leads to an open conformation, which increases its substrate binding but reduces its autoantibody inhibition. This gain-of-function ADAMTS13 variant may be further explored for the management of TTP and perhaps other inflammatory and thrombotic disorders.
Authors
- Karen Vanhoorelbeke (ORCID: https://orcid.org/0000-0003-2288-8277)
- M Pino Gil
- Zhirong Chai
- Konstantine Halkidis (ORCID: https://orcid.org/0000-0002-9594-1852)
- Chan Meng
- Quintijn Bonnez (ORCID: https://orcid.org/0000-0001-7209-530X)
- Szumam Liu
- Xiaxin Dong
- X. Long Zheng
Institutions
- Research Institute for Chromatography (BE)
- University of Kansas Medical Center (US)
Publication Details
- Journal
- Journal of Thrombosis and Haemostasis
- Published
- 2026-03-01
- DOI
- https://doi.org/10.1016/j.jtha.2026.03.010
- Primary Topic
- Complement system in diseases
- Type
- article
- Field-Weighted Citation Impact
- 0.00