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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
High-resolution structures of the IgM Fc domains reveal principles of its hexamer formation.
Proc. Natl. Acad. Sci. U.S.A. 110, 10183-10188 (2013)
IgM is the first antibody produced during the humoral immune response. Despite its fundamental role in the immune system, IgM is structurally only poorly described. In this work we used X-ray crystallography and NMR spectroscopy to determine the atomic structures of the constant IgM Fc domains (Cµ2, Cµ3, and Cµ4) and to address their roles in IgM oligomerization. Although the isolated domains share the typical Ig fold, they differ substantially in dimerization properties and quaternary contacts. Unexpectedly, the Cµ4 domain and its C-terminal tail piece are responsible and sufficient for the specific polymerization of Cµ4 dimers into covalently linked hexamers of dimers. Based on small angle X-ray scattering data, we present a model of the ring-shaped Cµ4 structure, which reveals the principles of IgM oligomerization.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
antibody oligomerization; dimer interfaces; hybrid approach; Mouse Immunoglobulin-m ; Crystal-structure ; Polymeric Structure ; Secretory Igm ; Chain ; Conformation ; Biogenesis ; Scattering ; Cysteine ; Erp44
ISSN (print) / ISBN
0027-8424
e-ISSN
1091-6490
Quellenangaben
Volume: 110,
Issue: 25,
Pages: 10183-10188
Publisher
National Academy of Sciences
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)