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- W2122075336 abstract "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 ligand C3b. The data suggest that C3b binding displaces the three N-terminal control domains and reshuffles the two central helices. Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain. This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response." @default.
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- W2122075336 date "2007-02-25" @default.
- W2122075336 modified "2023-10-16" @default.
- W2122075336 title "Factor B structure provides insights into activation of the central protease of the complement system" @default.
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- W2122075336 doi "https://doi.org/10.1038/nsmb1210" @default.
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