Abstract
The human type I allergic response is characterized by the presence of allergen-specific serum immunoglobulin E (IgE). Allergen-mediated cross-linking of receptor-bound IgE on the surface of mast cells and circulating basophils triggers the release of mediators, resulting in the development of the clinical symptoms of allergy. In order to study the structural basis of allergen-antibody interaction, a complex between the major birch-pollen allergen Bet v 1 and a Fab' fragment isolated from the murine monoclonal Bet v 1 antibody BV16 has been crystallized. Complex crystals belong to space group P1, with unit-cell parameters a = 91.65, b = 99.14, c = 108.90 A, alpha = 105.7, beta = 98.32, gamma = 97.62 degrees, and diffract to 2.9 A resolution when analyzed at 100 K using synchrotron-generated X--rays.
| Original language | English |
|---|---|
| Journal | Acta Crystallographica. Section D: Biological Crystallography |
| Volume | 55 |
| Issue number | Pt 12 |
| Pages (from-to) | 2035-6 |
| Number of pages | 2 |
| ISSN | 0907-4449 |
| Publication status | Published - Dec 1999 |
Keywords
- Allergens
- Animals
- Antibodies, Monoclonal
- Antigen-Antibody Reactions
- Antigens, Plant
- Crystallization
- Crystallography, X-Ray
- Humans
- Immunoglobulin Fab Fragments
- Immunoglobulin G
- Mice
- Plant Proteins
- Pollen
- Rhinitis, Allergic, Seasonal