Probing the molecular basis of allergy. Three-dimensional structure of the bovine lipocalin allergen Bos d 2

• Published in: The Journal of biological chemistry 1999-01, Vol.274 (4), p.2337-2343
• Main Authors: Rouvinen, J. (University of Joensuu, Joensuu, Finland.), Rautiainen, J, Virtanen, T, Zeiler, T, Kauppinen, J, Taivainen, A, Mantyjarvi, R
• Format: Article
• Language: English
• Subjects: ALERGENOS; ALLERGENE; ALLERGENS; Allergens - chemistry; Allergens - immunology; Amino Acid Sequence; ANALYTICAL METHODS; ANIMAL PROTEINS; Animals; ANTIGENE; ANTIGENOS; ANTIGENS; Antigens, Plant; BINDING SITES; BOVIN; Carrier Proteins - chemistry; Carrier Proteins - immunology; CATTLE; Crystallography, X-Ray; EPITOPES; GANADO BOVINO; GENERO HUMANO; GENRE HUMAIN; IGE; IMMUNOGLOBULINE; IMMUNOGLOBULINS; INMUNOGLOBULINA; MANKIND; MOLECULAR CONFORMATION; Molecular Probes; Molecular Sequence Data; PDB/1BJ7; Protein Conformation; PROTEINAS; PROTEINE; PROTEINS; Recombinant Proteins - chemistry; Recombinant Proteins - immunology; Sequence Homology, Amino Acid; TECHNIQUE ANALYTIQUE; TECNICAS ANALITICAS; X RAY DIFFRACTION
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.274.4.2337

The three-dimensional structure of the major bovine allergen Bos d 2 has been determined by using x-ray diffraction at 1.8-A resolution. Structurally Bos d 2 is a 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 binding. 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.