Probing the molecular basis of allergy. three-dimensional structure of the bovine lipocalin allergen Bos d 2.
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.
Rouvinen
J
J
Department of Chemistry, University of Joensuu, POB 111, FIN-80101 Joensuu, Finland. juha.rouvinen@joensuu.fi
Rautiainen
J
J
Virtanen
T
T
Zeiler
T
T
Kauppinen
J
J
Taivainen
A
A
Mäntyjärvi
R
R
D000485:Allergens / Q000737:chemistry* / Q000276:immunology; D000595:Amino Acid Sequence; D000818:Animals; D052179:Antigens, Plant; D002352:Carrier Proteins / Q000737:chemistry* / Q000276:immunology; D002417:Cattle; D018360:Crystallography, X-Ray; D015335:Molecular Probes; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000276:immunology; D017386:Sequence Homology, Amino Acid
D000485:Allergens; D052179:Antigens, Plant; C113339:Bos d 2 allergen; D002352:Carrier Proteins; D015335:Molecular Probes; D011994:Recombinant Proteins