A bovine dander allergen, comparative modeling, and similarities and differences in folding with related proteins
| Autor: | Rauno Mäntyjärvi, Harri Santa, Janne T. A. Saarela, Tuomas Virtanen, Jaakko Rautianen, Marja Rytkönen, Reino Laatikainen |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular Protein Folding Molecular Sequence Data Phenylalanine Lipocalin medicine.disease_cause Biochemistry Androgen-Binding Protein Protein Structure Secondary Epitope Allergen Alpha-Globulins medicine Animals Amino Acid Sequence Tyrosine Chemistry Glutamic acid Allergens Antigens Plant Small molecule Retinol-Binding Proteins Folding (chemistry) Cattle Carrier Proteins Sequence Alignment |
| Zdroj: | Journal of Protein Chemistry. 17:657-662 |
| ISSN: | 1573-4943 0277-8033 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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