2KPY
Solution Structure of the major allergen of Artemisia vulgaris (Art v 1)
Summary for 2KPY
| Entry DOI | 10.2210/pdb2kpy/pdb |
| NMR Information | BMRB: 16111 |
| Descriptor | Major pollen allergen Art v 1 (1 entity in total) |
| Functional Keywords | defensin-like, poly-proline, allergen |
| Biological source | Artemisia vulgaris (common wormwood) |
| Total number of polymer chains | 1 |
| Total formula weight | 10816.04 |
| Authors | Razzera, G.,Gadermaier, G.,Almeida, M.,Egger, M.,Jahn-Schmid, B.,Almeida, F.,Ferreira, F.,Valente, A. (deposition date: 2009-10-23, release date: 2010-10-06, Last modification date: 2023-06-14) |
| Primary citation | Razzera, G.,Gadermaier, G.,de Paula, V.,Almeida, M.S.,Egger, M.,Jahn-Schmid, B.,Almeida, F.C.,Ferreira, F.,Valente, A.P. Mapping the interactions between a major pollen allergen and human IgE antibodies. Structure, 18:1011-1021, 2010 Cited by PubMed Abstract: The interaction of specific IgE antibodies with allergens is a key event in the induction of allergic symptoms, thus representing an important target for therapeutic interventions in Type I allergies. We report here the solution NMR structure of Art v 1, the major mugwort pollen allergen. Art v 1 is the first protein structure with an allergenic defensin fold linked to a polyproline domain, which has not been identified in any reported allergen structure in the PDB. Moreover, the direct interaction of polyclonal IgE antibodies from an allergic patient has been mapped on the surface of an allergen for the first time. The data presented herein provide the basis for the design of tools for safe and effective vaccination against mugwort pollen allergy. PubMed: 20696401DOI: 10.1016/j.str.2010.05.012 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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