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A molecular basis for von Willebrand factor (VWF) self‐inhibition has been proposed by which the N‐terminal and C‐terminal flanking sequences of the globular A1 domain disulfide loop bind to and… Click to show full abstract
A molecular basis for von Willebrand factor (VWF) self‐inhibition has been proposed by which the N‐terminal and C‐terminal flanking sequences of the globular A1 domain disulfide loop bind to and suppress the conformational dynamics of A1. These flanking sequences are rich in O‐linked glycosylation (OLG), which is known to suppress platelet adhesion to VWF, presumably by steric hindrance. The inhibitory mechanism remains unresolved as to whether inhibition is due to steric exclusion by OLGs or a direct self‐association interaction that stabilizes the domain.
Journal Title: Journal of Thrombosis and Haemostasis
Year Published: 2019
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