6Y3K

NMR solution structure of the hazelnut allergen Cor a 1.0403

6Y3K の概要

• エントリーDOI: 10.2210/pdb6y3k/pdb
• NMR情報: BMRB: 27967
• 分子名称: Major allergen variant Cor a 1.0403 (1 entity in total)
• 機能のキーワード: pr-10 protein, hazelnut allergen, bet v 1 cross reactive protein, allergen
• 由来する生物種: Corylus avellana (European hazel)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17420.83

構造登録者

Fuehrer, S.,Kamenik, A.S.,Zeindl, R.,Nothegger, B.,Hofer, F.,Reider, N.,Liedl, K.R.,Tollinger, M. (登録日: 2020-02-18, 公開日: 2021-02-17, 最終更新日: 2024-06-19)

主引用文献

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

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: 33603065
DOI: 10.1038/s41598-021-83705-z

実験手法

SOLUTION NMR