ArticleProceedings of the National Academy of Sciences of the United States of America2009
Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 159 citations in OpenAlex.
- Residues Arg568 and Phe592 contribute to an antigenic surface for anti-ADAMTS13 antibodies in the spacer domain.Haematologica · 2011Trial
- Crystal structure of a β1,3-Glucosyltransferase reveals an unusual substrate recognition by a two-domain GT-A fold glycosyltransferase.The Journal of biological chemistry · 2026Article
- Longitudinal multiomics profiling of extracorporeal cross-circulation with pig liver xenografts in human decedents.Nature medicine · 2026Article
- Novel cryptic ADAMTS13 epitopes uncover a distinct open ADAMTS13 conformation in immune-mediated TTP.Haematologica · 2026Article
- ADAMTS13 as a thromboinflammatory brake at the vascular-immune interface: from viral immunothrombosis to the tumor microenvironment.Frontiers in immunology · 2026Review
- Deep molecular modeling and mechanistic insights into type 2A von Willebrand disease with von Willebrand factor A2 domain mutations.Research and practice in thrombosis and haemostasis · 2025Article
- Open or closed? Understanding the molecular mechanisms and clinical implications of ADAMTS13's conformation.HemaSphere · 2025Review
- A Disintegrin and Metalloprotease with Thrombospondin Motif, Member 13, and Von Willebrand Factor in Relation to the Duality of Preeclampsia and HIV Infection.International journal of molecular sciences · 2025Review
- A Novel P-III Metalloproteinase fromToxins · 2024Article
- Mechanisms of ADAMTS13 regulation.Journal of thrombosis and haemostasis : JTH · 2022Review
- Targeting Aggrecanases for Osteoarthritis Therapy: From Zinc Chelation to Exosite Inhibition.Journal of medicinal chemistry · 2022Review
- ADAMTS13 conformations and mechanism of inhibition in immune thrombotic thrombocytopenic purpura.Journal of thrombosis and haemostasis : JTH · 2022Review
- Synonymous ADAMTS13 variants impact molecular characteristics and contribute to variability in active protein abundance.Blood advances · 2022Article
- O-fucosylation stabilizes the TSR3 motif in thrombospondin-1 by interacting with nearby amino acids and protecting a disulfide bond.The Journal of biological chemistry · 2022Article
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- The polymorphisms of extracellular matrix-remodeling genes are associated with pelvic organ prolapse.International urogynecology journal · 2022Article
- Residues R1075, D1090, R1095, and C1130 Are Critical in ADAMTS13 TSP8-Spacer Interaction Predicted by Molecular Dynamics Simulation.Molecules (Basel, Switzerland) · 2021Article
- Exposure of Von Willebrand Factor Cleavage Site in A1A2A3-Fragment under Extreme Hydrodynamic Shear.Polymers · 2021Article
- Article
- Crystal structure of ADAMTS13 CUB domains reveals their role in global latency.Science advances · 2021Article
17 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADAMTS13 specifically cleaves plasma von Willebrand factor (VWF) and thereby controls VWF-mediated platelet thrombus formation. Severe deficiencies in ADAMTS13 can cause life-threatening thrombotic thrombocytopenic purpura. Here, we determined 2 crystal structures of ADAMTS13-DTCS (residues 287-685), an exosite-containing human ADAMTS13 fragment, at 2.6-A and 2.8-A resolution. The structures revealed folding similarities between the disintegrin-like (D) domain and the N-terminal portion of the cysteine-rich domain (designated the C(A) domain). The spacer (S) domain forms a globular functional unit with a 10-stranded beta-sandwich fold that has multiple interaction sites with the C(A) domain. We expressed 25 structure-based mutants of ADAMTS13-MDTCS (residues 75-685) and measured their enzymatic activity. We identified 3 VWF-binding exosites on the linearly aligned discontinuous surfaces of the D, C(A), and S domains traversing the W-shaped molecule. Since the MDTCS domains are conserved among ADAMTS family proteins, the structural framework of the multiple enzyme-substrate interactions identified in the ADAMTS13-VWF system provides the basis for a common substrate recognition mode in this class of proteinases.
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