4.6 Article

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

期刊

IMMUNOLOGY
卷 126, 期 3, 页码 378-385

出版社

WILEY
DOI: 10.1111/j.1365-2567.2008.02904.x

关键词

Fc fragment; glycosylation; immune complex; immunoglobulin; saccharides; X-ray structure

资金

  1. Ministry of Education, Youth and Sports of the Czech Republic [1K05008]
  2. Grant Agency of the Academy of Sciences of the Czech Republic [IAA500500701]
  3. European Commission [031220]

向作者/读者索取更多资源

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 angstrom 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.

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