PuSH - Publikationsserver des Helmholtz Zentrums München

Müller, R.* ; Gräwert, M.A.* ; Kern, T. ; Madl, T. ; Peschek, J.* ; Sattler, M. ; Groll, M.* ; Buchner, J.*

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)
Verlagsversion Volltext DOI
Free by publisher
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.
Weitere Metriken?
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter 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 Band: 110, Heft: 25, Seiten: 10183-10188 Artikelnummer: , Supplement: ,
Verlag National Academy of Sciences
Begutachtungsstatus Peer reviewed