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

被引：24

作者：

Kolenko, Petr ^{[1
]}

Dohnalek, Jan ^{[1
]}

Duskova, Jarmila ^{[1
]}

Skalova, Tereza ^{[1
]}

Collard, Renata ^{[2
]}

Hasek, Jindrich ^{[1
]}

机构：

[1] Acad Sci Czech Republ, Inst Macromol Chem, Dept Struct Anal, CR-16206 Prague 6, Czech Republic

[2] Univ Colorado, Hlth Sci Ctr, Dept Pediat, Aurora, CO USA

来源：

IMMUNOLOGY | 2009年 / 126卷 / 03期

关键词：

Fc fragment; glycosylation; immune complex; immunoglobulin; saccharides; X-ray structure; MEDIATED IMMUNE PRECIPITATION; FC FRAGMENT; COMPLEX; REFINEMENT; PROGRAM; BINDING; SITE;

D O I：

10.1111/j.1365-2567.2008.02904.x

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

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.

引用

页码：378 / 385

页数：8

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