A BOVINE DANDER ALLERGEN, COMPARATIVE MODELING, AND SIMILARITIES AND DIFFERENCES IN FOLDING WITH RELATED PROTEINS

The most important allergenic protein in cow dander and urine is Bos d 2. It is proposed to belong to the family of lipocalins, which are pr oteins capable of binding small hydrophobic molecules. The allergenic properties of Bos d 2 indicate an interaction between the accessible r egions of the native protein and IgE. In this work, a three-dimensiona l model was created for Bos d 2 by comparative modeling, and features characteristic of outlier lipocalins were observed. The protruding reg ions of the surface were characterized and used in predicting the poss ible B-cell epitopes. There is a pocket inside the core and its size i s appropriate for small molecules. The model shows a hydrophilic amino acid side chain of glutamic acid 115 on the inner surface of the hole and a phenylalanine as the ''gatekeeper'' instead of tyrosine, which is common in experimentally modeled lipocalins.