Structural specializations of A 2 , a force-sensing domain in the ultralarge vascular protein von Willebrand factor

@inproceedings{Zhang2009StructuralSO,
  title={Structural specializations of A 2 , a force-sensing domain in the ultralarge vascular protein von Willebrand factor},
  author={Qing Zhang and Yan-Feng Zhou and Cheng-Zhong Zhang and Xiaohui Zhang and Chafen Lu and Timothy A Springer},
  year={2009}
}
The lengths of von Willebrand factor (VWF) concatamers correlate with hemostatic potency. After secretion in plasma, length is regulated by hydrodynamic shear force-dependent unfolding of the A2 domain, which is then cleaved by a specific protease. The 1.9-Å crystal structure of the A2 domain demonstrates evolutionary adaptations to this shear sensor function. Unique among VWF A (VWA) domains, A2 contains a loop in place of the 4 helix, and a cis-proline. The central 4-strand is poorly packed… CONTINUE READING
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