6Z98
NMR solution structure of the peach allergen Pru p 1.0101
Summary for 6Z98
| Entry DOI | 10.2210/pdb6z98/pdb |
| NMR Information | BMRB: 27687 |
| Descriptor | Major allergen Pru p 1 (1 entity in total) |
| Functional Keywords | peach pru p 1 food allergen, pathogenesis related protein, cross-allergy, allergen |
| Biological source | Prunus persica (Peach) |
| Total number of polymer chains | 1 |
| Total formula weight | 17542.63 |
| Authors | Eidelpes, R.,Fuehrer, S.,Hofer, F.,Kamenik, A.S.,Liedl, K.R.,Tollinger, M. (deposition date: 2020-06-03, release date: 2021-06-30, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 34260238DOI: 10.1021/acs.jafc.1c01876 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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