A common mechanism by which type 2A von Willebrand disease mutations enhance ADAMTS13 proteolysis revealed with a von Willebrand factor A2 domain FRET construct

Rheological forces in the blood trigger the unfolding of von Willebrand factor (VWF) and its A2 domain, exposing the scissile bond for proteolysis by ADAMTS13. Under quiescent conditions, the scissile bond is hidden by the folded structure due to the stabilisation provided by the structural speciali...

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Detalles Bibliográficos
Autores principales: Lynch, Christopher J., Cawte, Adam D., Millar, Carolyn M., Rueda, David, Lane, David A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5706690/
https://www.ncbi.nlm.nih.gov/pubmed/29186156
http://dx.doi.org/10.1371/journal.pone.0188405

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5706690/
https://www.ncbi.nlm.nih.gov/pubmed/29186156
http://dx.doi.org/10.1371/journal.pone.0188405

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