6Z98

NMR solution structure of the peach allergen Pru p 1.0101

6Z98 の概要

• エントリーDOI: 10.2210/pdb6z98/pdb
• NMR情報: BMRB: 27687
• 分子名称: Major allergen Pru p 1 (1 entity in total)
• 機能のキーワード: peach pru p 1 food allergen, pathogenesis related protein, cross-allergy, allergen
• 由来する生物種: Prunus persica (Peach)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17542.63

構造登録者

Eidelpes, R.,Fuehrer, S.,Hofer, F.,Kamenik, A.S.,Liedl, K.R.,Tollinger, M. (登録日: 2020-06-03, 公開日: 2021-06-30, 最終更新日: 2024-05-15)

主引用文献

Eidelpes, R.,Hofer, F.,Rock, M.,Fuhrer, S.,Kamenik, A.S.,Liedl, K.R.,Tollinger, M.
Structure and Zeatin Binding of the Peach Allergen Pru p 1 .
J.Agric.Food Chem., 69:8120-8129, 2021

PubMed Abstract: Peach () is among the fruits most frequently reported to cause food allergies. Allergic reactions commonly result from previous sensitization to the birch pollen allergen Bet v 1, followed by immunological cross-reactivity of IgE antibodies to structurally related proteins in peach. In this study, we present the three-dimensional NMR solution structure of the cross-reactive peach allergen (isoform Pru p 1.0101). This 17.5 kDa protein adopts the canonical Bet v 1 fold, composed of a seven-stranded β-sheet and three α-helices enclosing an internal cavity. In , the inner surface of the cavity contains an array of hydroxyl-bearing amino acids surrounded by a hydrophobic patch, constituting a docking site for amphiphilic molecules. NMR-guided docking of the cytokinin molecule zeatin to the internal cavity of provides a structure-based rationale for the effect that zeatin binding has on the protein's RNase activity.

PubMed: 34260238
DOI: 10.1021/acs.jafc.1c01876

実験手法

SOLUTION NMR