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 proteins capable of binding small hydrophobic molecules. The allergenic properties of Bos d 2 indicate an interaction between the accessible regions of the native protein and IgE. In this work, a three-dimensional model was created for Bos d 2 by comparative modeling, and features characteristic of outlier lipocalins were observed. The protruding regions of the surface were characterized and used in predicting the possible B-cell epitopes. There is a pocket inside the core and its size is 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.
Santa
H
H
Department of Chemistry, University of Kuopio, Finland. santa@kummeli.uku.fi
Saarela
J T
JT
Laatikainen
R
R
Rautianen
J
J
Virtanen
T
T
Rytkönen
M
M
Mäntyjärvi
R
R
D000485:Allergens / Q000737:chemistry*; D000510:Alpha-Globulins / Q000737:chemistry; D000595:Amino Acid Sequence; D000727:Androgen-Binding Protein / Q000737:chemistry; D000818:Animals; D052179:Antigens, Plant; D002352:Carrier Proteins / Q000737:chemistry*; D002417:Cattle; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012177:Retinol-Binding Proteins / Q000737:chemistry; D016415:Sequence Alignment
D000485:Allergens; D000510:Alpha-Globulins; D000727:Androgen-Binding Protein; D052179:Antigens, Plant; C113339:Bos d 2 allergen; D002352:Carrier Proteins; D012177:Retinol-Binding Proteins; C027519:probasin