Article

Dynamic Disulfide Bond Topologies in von-Willebrand-Factor’s C4-Domain Undermine Platelet Binding

2022-08-21

Abstract excerpt

<h4>Summary</h4> <h4>Background</h4> The von Willebrand Factor (vWF) is a key player in regulating hemostasis through adhesion of platelets to sites of vascular injury. It is a large multi-domain mechano-sensitive protein stabilized by a net of disulfide bridges. Binding to platelet integrin is achieved by the vWF-C4 domain which exhibits a fixed fold, even under conditions of severe mechanical stress, but only...

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Literature Corpus work: 9fb6ce51-ab9c-5ce9-bdea-a241ff61aa59
DOI: 10.1101/2022.08.20.504523

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