Factor B structure provides insights into activation of the central protease of the complement system

@article{Milder2007FactorBS,
  title={Factor B structure provides insights into activation of the central protease of the complement system},
  author={Fin J. Milder and L{\'u}cio de Moura Gomes and A. R. Schouten and Bert J.C. Janssen and Eric G Huizinga and R. Romijn and Wieger Hemrika and Anja Roos and Mohamed R. Daha and Piet Gros},
  journal={Nature Structural &Molecular Biology},
  year={2007},
  volume={14},
  pages={224-228}
}
Factor B is the central protease of the complement system of immune defense. Here, we present the crystal structure of human factor B at 2.3-Å resolution, which reveals how the five-domain proenzyme is kept securely inactive. The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker. The two helices conformationally link the scissile-activation peptide and the metal ion–dependent adhesion site required for binding of the… CONTINUE READING
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