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Article

A discontinuous autoinhibitory module masks the A1 domain of von Willebrand factor.

Journal of thrombosis and haemostasis : JTH - 1 Sept 2017

Deng W, Wang Y, Druzak S A, Healey J F, Syed A K, Lollar P, Li R

Abstract excerpt

Essentials The mechanism for the auto-inhibition of von Willebrand factor (VWF) remains unclear. Hydrogen exchange of two VWF A1 fragments with disparate activities was measured and compared. Discontinuous residues flanking A1 form a structural module that blocks A1 binding to the platelet. Our results suggest a potentially unified model of VWF activation. Click to hear an ISTH Academy presentation on the domain...

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Topics

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Share to Blood Platelets
Share to Binding, Competitive
Share to Deuterium Exchange Measurement

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Platelet Glycoprotein GPIb-IX Complex

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Share to von Willebrand Factor

Source

Open in PubMed Open full text

Identifiers

PMID: 28692141
DOI: 10.1111/jth.13775
PMCID: PMC5585049

Genes

VWF
HDX

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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