Physical Chemistry Chemical Physics
Article . 2022 . Peer-reviewed
License: Royal Society of Chemistry Licence to Publish
Data sources: Crossref
The soluble N-terminal autoinhibitory module of the A1 domain in von Willebrand factor partially suppresses its catch bond with glycoprotein Ibα in a sandwich complex
ARC| Discovery Projects - Grant ID: DP200101970 ,
ARC| Discovery Early Career Researcher Award - Grant ID: DE190100609
Authors: Yunduo Charles Zhao; Zhenhai Li; Lining Arnold Ju;
doi: 10.1039/d2cp01581a
pmid: 35698887
The soluble N-terminal autoinhibitory module of the A1 domain in von Willebrand factor partially suppresses its catch bond with glycoprotein Ibα in a sandwich complex
Abstract
The von Willebrand factor A1 domain-derived polypeptide sequence Q1238-E1260 forms a hairpin-like structure in trans. Soluble Q1238-E1260 partially inhibits A1–GPIbα binding while retaining its catch-bond behavior in a sandwich complex.
Related Organizations
- Georgia Institute of Technology United States
- Shanghai University China (People's Republic of)
- The Heart Research Institute Australia
- University of Sydney Australia
- Emory University United States
Keywords
Blood Platelets, Molecular Docking Simulation, Platelet Glycoprotein GPIb-IX Complex, von Willebrand Factor, COVID-19, Humans, Protein Binding
Blood Platelets, Molecular Docking Simulation, Platelet Glycoprotein GPIb-IX Complex, von Willebrand Factor, COVID-19, Humans, Protein Binding
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This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
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