4JVW

IgM C4-domain from mouse

Summary for 4JVW

• Entry DOI: 10.2210/pdb4jvw/pdb
• Related: 4JVU
• Descriptor: Ig mu chain C region secreted form (2 entities in total)
• Functional Keywords: immunoglobulin m, antibody, oligomerization, immunoglobulin fold, receptor, protein binding
• Biological source: Mus musculus (mouse)
• Cellular location: Secreted (Probable): P01872
• Total number of polymer chains: 4
• Total formula weight: 50973.66

Authors

Mueller, R.,Graewert, A.M.,Kern, T.,Madl, T.,Peschek, J.,Sattler, M.,Groll, M.,Buchner, J. (deposition date: 2013-03-26, release date: 2013-06-12, Last modification date: 2024-10-16)

Primary citation

Muller, R.,Grawert, 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.USA, 110:10183-10188, 2013

PubMed 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.

PubMed: 23733956
DOI: 10.1073/pnas.1300547110

Experimental method

X-RAY DIFFRACTION (2 Å)