Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Müller, R; Gräwert, MA; 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. 2013; 110(25): 10183-10188.
Doi: 10.1073/pnas.1300547110
[OPEN ACCESS]
Web of Science
PubMed
FullText
FullText_MUG
- Co-Autor*innen der Med Uni Graz
- Madl Tobias
- Altmetrics:
- Dimensions Citations:
- Plum Analytics:
- Scite (citation analytics):
- Abstract:
- 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.
- Find related publications in this database (using NLM MeSH Indexing)
- Crystallography, X-Ray -
- Dimerization -
- Humans -
- Immunoglobulin Fc Fragments - chemistry
- Immunoglobulin M - chemistry
- Models, Molecular -
- Nuclear Magnetic Resonance, Biomolecular -
- Polymerization -
- Protein Structure, Quaternary -
- Protein Structure, Tertiary -
- Recombinant Proteins - chemistry
- Structure-Activity Relationship -
- Find related publications in this database (Keywords)
- antibody oligomerization
- hybrid approach
- dimer interfaces