6Y3K
NMR solution structure of the hazelnut allergen Cor a 1.0403
Summary for 6Y3K
| Entry DOI | 10.2210/pdb6y3k/pdb |
| NMR Information | BMRB: 27967 |
| Descriptor | Major allergen variant Cor a 1.0403 (1 entity in total) |
| Functional Keywords | pr-10 protein, hazelnut allergen, bet v 1 cross reactive protein, allergen |
| Biological source | Corylus avellana (European hazel) |
| Total number of polymer chains | 1 |
| Total formula weight | 17420.83 |
| Authors | Fuehrer, S.,Kamenik, A.S.,Zeindl, R.,Nothegger, B.,Hofer, F.,Reider, N.,Liedl, K.R.,Tollinger, M. (deposition date: 2020-02-18, release date: 2021-02-17, Last modification date: 2024-06-19) |
| Primary citation | Fuhrer, S.,Kamenik, A.S.,Zeindl, R.,Nothegger, B.,Hofer, F.,Reider, N.,Liedl, K.R.,Tollinger, M. Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens. Sci Rep, 11:4173-4173, 2021 Cited by PubMed Abstract: A major proportion of allergic reactions to hazelnuts (Corylus avellana) are caused by immunologic cross-reactivity of IgE antibodies to pathogenesis-related class 10 (PR-10) proteins. Intriguingly, the four known isoforms of the hazelnut PR-10 allergen Cor a 1, denoted as Cor a 1.0401-Cor a 1.0404, share sequence identities exceeding 97% but possess different immunologic properties. In this work we describe the NMR solution structures of these proteins and provide an in-depth study of their biophysical properties. Despite sharing highly similar three-dimensional structures, the four isoforms exhibit remarkable differences regarding structural flexibility, hydrogen bonding and thermal stability. Our experimental data reveal an inverse relation between structural flexibility and IgE-binding in ELISA experiments, with the most flexible isoform having the lowest IgE-binding potential, while the isoform with the most rigid backbone scaffold displays the highest immunologic reactivity. These results point towards a significant entropic contribution to the process of antibody binding. PubMed: 33603065DOI: 10.1038/s41598-021-83705-z PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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