Structures of C1-IgG1 provide insights into how danger pattern recognition activates complement-Reference-Cited by-同舟云学术

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

Published:2018-02-16 Issue:6377 Volume:359 Page:794-797
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Ugurlar Deniz¹^ORCID,Howes Stuart C.²^ORCID,de Kreuk Bart-Jan³,Koning Roman I.²⁴^ORCID,de Jong Rob N.³^ORCID,Beurskens Frank J.³^ORCID,Schuurman Janine³^ORCID,Koster Abraham J.²⁴^ORCID,Sharp Thomas H.²^ORCID,Parren Paul W. H. I.³⁵^ORCID,Gros Piet¹^ORCID

Affiliation:

1. Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands.

2. Section of Electron Microscopy, Department of Molecular Cell Biology, Leiden University Medical Center, Einthovenweg 20, 2300 RC Leiden, Netherlands.

3. Genmab, Yalelaan 60, 3584 CM Utrecht, Netherlands.

4. NeCEN, Gorlaeus Laboratories, Leiden University, 2333 CC Leiden, Netherlands.

5. Department of Immunohematology and Blood Transfusion, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, Netherlands.

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

Funder

European Research Council

Netherlands Organization for Scientific Research

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference47 articles.

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