Structures of C1-IgG1 provide insights into how danger pattern recognition activates complement | Zendy

Deniz Ugurlar | Zendy; Stuart C. Howes | Zendy; Bart-Jan de Kreuk | Zendy; Roman I. Koning | Zendy; Rob N. de Jong | Zendy; Frank J. Beurskens | Zendy; Janine Schuurman | Zendy; Abraham J. Koster | Zendy; Thomas H. Sharp | Zendy; Paul W.H.I. Parren | Zendy; Piet Gros | Zendy

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Structures of C1-IgG1 provide insights into how danger pattern recognition activates complement

Author(s) -

Deniz Ugurlar,

Stuart C. Howes,

Bart-Jan de Kreuk,

Roman I. Koning,

Rob N. de Jong,

Frank J. Beurskens,

Janine Schuurman,

Abraham J. Koster,

Thomas H. Sharp,

Paul W.H.I. Parren,

Piet Gros

Publication year - 2018

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aao4988

Subject(s) - random hexamer , avidity , antibody , immune system , classical complement pathway , mutagenesis , complement system , microbiology and biotechnology , immune recognition , biology , complement (music) , immunoglobulin g , chemistry , biophysics , immunology , genetics , mutation , mutant , complementation , gene

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. Ugurlaret 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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