New insights into intra- and intermolecular interactions of immunoglobulins: crystal structure of mouse IgG2b-Fc at 2.1-A resolution

The structure of the Fc fragment of monoclonal antibody IgG2b from hybridom M75 of Mus musculus has been determined by single crystal X-ray diffraction. This is the first report of the structure of the murine immunoglobulin isotype IgG2b. The structure refined at 2.1 A resolution provides more detai...

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Bibliographic Details
Published in:Immunology 2009-03, Vol.126 (3), p.378-385
Main Authors: Kolenko, Petr, Dohnálek, Jan, Dusková, Jarmila, Skálová, Tereza, Collard, Renata, Hasek, Jindrich
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal - chemistry
Antigen-Antibody Complex - chemistry
Crystallization
Crystallography, X-Ray - methods
Glycosylation
Immunoglobulin Fc Fragments - chemistry
Immunoglobulin G - chemistry
Mice
Oligosaccharides - chemistry
Protein Structure, Secondary
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Summary:The structure of the Fc fragment of monoclonal antibody IgG2b from hybridom M75 of Mus musculus has been determined by single crystal X-ray diffraction. This is the first report of the structure of the murine immunoglobulin isotype IgG2b. The structure refined at 2.1 A resolution provides more detailed structural information about native oligosaccharides than was previously available. High-quality Fourier maps provide a clear identification of alpha-l-fucose with partial occupancy in the first branch of the antennary oligosaccharides. A unique Fc:Fc interaction was observed at the C(H)2-C(H)3 interface.
ISSN:1365-2567
DOI:10.1111/j.1365-2567.2008.02904.x