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

P. Kolenko, J. Dohnálek, J. Dušková, T. Skálová, R. Collard, J. Hašek

. 2009 ; 126 (3) : 378-385.

Jazyk angličtina Země Velká Británie

Perzistentní odkaz   https://www.medvik.cz/link/bmc11009513
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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.

Citace poskytuje Crossref.org

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