Structures of C1-IgG1 provide insights into how danger pattern recognition activates complement
Deniz Ugurlar(Utrecht University), Stuart C. Howes(Leiden University Medical Center), Bart-Jan de Kreuk(Genmab (Netherlands)), Roman I. Koning(Leiden University), Rob N. de Jong(Genmab (Netherlands)), Frank J. Beurskens(Genmab (Netherlands)), Janine Schuurman(Genmab (Netherlands)), Abraham J. Koster(Leiden University), Thomas H. Sharp(Leiden University Medical Center), Paul W.H.I. Parren(Leiden University Medical Center), Piet Gros(Utrecht University)
Cited by 186
Abstract
Recognizing danger signals In the classical complement pathway, the C1 initiation complex binds to danger patterns on the surface of microbes or damaged host cells and triggers an immune response. Immunoglobulin G (IgG) antibodies form hexamers on cell surfaces that have high avidity for the C1 complex. Ugurlar et al. used cryo–electron microscopy to show how a hexamer of C1 complexes interacts with the IgG hexamer. Structure-guided mutagenesis revealed how C1 is activated to trigger an immune response. Science , this issue p. 794
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