The three-dimensional structure of the major bovine allergen Bos d 2 has been determined by using x-ray diffraction at 1.8-Å resolution. Structurally Bosd2isa member of the lipocalin family comprising proteins with transport functions. There is a flat small cavity inside the Bos d 2 protein core suitable for ligand binding, and it is possible that Glu115 and Asn37 inside the core are able to make hydrogen bonds with the ligand. Many allergens from different animals belong to the lipocalin family. The amino acid residue similarities between these lipocalins indicate putative regions for IgE bind- ing. Comparison with the available allergen structures from other sources suggests that these allergens are roughly the same size and that their shape is more spherical than elliptical.
CITATION STYLE
Rouvinen, J., Rautiainen, J., Virtanen, T., Zeiler, T., Kauppinen, J., Taivainen, A., & Mäntyjärvi, R. (1999). Probing the Molecular Basis of Allergy. Journal of Biological Chemistry, 274(4), 2337–2343. https://doi.org/10.1074/jbc.274.4.2337
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