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New insights into intra- and intermolecular interactions of immunoglobulins: crystal structure of mouse IgG2b-Fc at 2.1-A resolution
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SYSNO ASEP 0321119 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title New insights into intra- and intermolecular interactions of immunoglobulins: crystal structure of mouse IgG2b-Fc at 2.1-A resolution Title Nové náhledy na intra- a intermolekulární interakce imunoglobulinů: krystalová struktura myšího IgG2b-Fc s rozlišením 2.1-A Author(s) Kolenko, Petr (UMCH-V) RID
Dohnálek, Jan (UMCH-V) RID
Dušková, Jarmila (UMCH-V) RID
Skálová, Tereza (UMCH-V) RID
Collard, R. (US)
Hašek, Jindřich (UMCH-V) RIDSource Title Immunology - ISSN 0019-2805
Roč. 126, č. 126 (2009), s. 378-385Number of pages 8 s. Language eng - English Country GB - United Kingdom Keywords immunoglobulin ; Fc-fragment ; glycosylation Subject RIV CD - Macromolecular Chemistry R&D Projects 1K05008 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z40500505 - UMCH-V (2005-2011) UT WOS 000263038700009 DOI 10.1111/j.1365-2567.2008.02904.x Annotation 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 α-L-fucose with partial occupancy in the first branch of the antennary oligosaccharides. A unique Fc:Fc interaction was observed at the CH2-CH3 interface. Workplace Institute of Macromolecular Chemistry Contact Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Year of Publishing 2009
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