New insights into intra- and intermolecular interactions of immunoglobulins: crystal structure of mouse IgG2b-Fc at 2.1-A resolution
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
18783468
PubMed Central
PMC2669818
DOI
10.1111/j.1365-2567.2008.02904.x
PII: IMM2904
Knihovny.cz E-zdroje
- MeSH
- glykosylace MeSH
- imunoglobulin G chemie MeSH
- imunoglobuliny - Fc fragmenty chemie MeSH
- imunokomplex chemie MeSH
- krystalizace MeSH
- krystalografie rentgenová metody MeSH
- monoklonální protilátky chemie MeSH
- myši MeSH
- oligosacharidy chemie MeSH
- sekundární struktura proteinů MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- imunoglobulin G MeSH
- imunoglobuliny - Fc fragmenty MeSH
- imunokomplex MeSH
- monoklonální protilátky MeSH
- oligosacharidy MeSH
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.
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