Structural highlights
Function[ALL2_BOVIN] Probable pheromone carrier. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Probing the molecular basis of allergy. three-dimensional structure of the bovine lipocalin allergen Bos d 2.,Rouvinen J, Rautiainen J, Virtanen T, Zeiler T, Kauppinen J, Taivainen A, Mantyjarvi R J Biol Chem. 1999 Jan 22;274(4):2337-43. PMID:9891000[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References | ||||||||||||||||
This page was last modified 15:00, 9 February 2016.