Crystallization and preliminary X-ray diffraction analysis of two homologous antigen-binding fragments in complex with different carbohydrate antigens

Citation
Hp. Nguyen et al., Crystallization and preliminary X-ray diffraction analysis of two homologous antigen-binding fragments in complex with different carbohydrate antigens, ACT CRYST D, 57, 2001, pp. 1872-1876
Citations number
26
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
12
Pages
1872 - 1876
Database
ISI
SICI code
0907-4449(200112)57:<1872:CAPXDA>2.0.ZU;2-Y
Abstract
The antigen-binding fragments (Fab) of two murine monoclonal antibodies (mA b) S25-2 and S45-18, specific for carbohydrate epitopes in the lipopolysacc haide of the bacterial family Chlamydiaceae, have been crystallized in the presence and absence of synthetic oligosaccharides corresponding to their r espective haptens. Crystals of both Fabs show different morphology dependin g on the presence of antigens. The sequence of mAb S45-18 was determined an d shows a remarkable homology to that reported for mAb S25-2. These crystal s offer an unparalleled opportunity to compare the structure and modes of b inding of two homologous antibodies to similar but distinct carbohydrate ep itopes.