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Structural Origins of Misfolding Propensity in the Platelet Adhesive Von Willebrand Factor A1 Domain
The von Willebrand factor (VWF) A1 and A3 domains are structurally isomorphic yet exhibit distinct mechanisms of unfolding. The A1 domain, responsible for platelet adhesion to VWF in hemostasis, unfolds through a molten globule intermediate in an apparent three-state mechanism, while A3 unfolds by a...
Tallennettuna:
| Julkaisussa: | Biophys J |
|---|---|
| Päätekijät: | , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
The Biophysical Society
2015
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4621621/ https://ncbi.nlm.nih.gov/pubmed/26200876 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2015.06.008 |
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