Structural origins of misfolding propensity in the platelet adhesive von Willebrand factor A1 domain.

@article{Zimmermann2015StructuralOO,
  title={Structural origins of misfolding propensity in the platelet adhesive von Willebrand factor A1 domain.},
  author={Michael T. Zimmermann and Alexander Tischer and Steven T. Whitten and Matthew Auton},
  journal={Biophysical journal},
  year={2015},
  volume={109 2},
  pages={398-406}
}
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 classical two-state mechanism. Inspection of the sequences or structures alone does not elucidate the source of this thermodynamic conundrum; however, the three-state character of the A1 domain… CONTINUE READING

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