8QHH
NMR solution structure of the green kiwi fruit allergen Act d 8.0101
Summary for 8QHH
Entry DOI | 10.2210/pdb8qhh/pdb |
NMR Information | BMRB: 50811,50812 |
Descriptor | Bet v 1 related allergen (1 entity in total) |
Functional Keywords | pr-10 allergen, allergen |
Biological source | Actinidia deliciosa |
Total number of polymer chains | 1 |
Total formula weight | 16812.11 |
Authors | |
Primary citation | Zeindl, R.,Tollinger, M. NMR resonance assignments of the PR-10 allergens Act c 8 and Act d 8 from golden and green kiwifruit. Biomol NMR Assign, 15:367-371, 2021 Cited by PubMed Abstract: Kiwifruits have become one of the most common food sources triggering allergic reactions. In patients suffering from birch pollen related food allergy, reactions result from initial sensitization to the birch (Betula verrucosa) pollen allergen Bet v 1, followed by immunological cross-reactivity to structurally homologous proteins in kiwifruit. Clinical symptoms range from scratching and itching of the oral cavity to more severe immunological reactions such as rhino conjunctivitis. In this work we assigned backbone and side chain H, C and N chemical shifts of the 17 kDa PR-10 allergens Act c 8.0101 and Act d 8.0101 from golden (Actinidia chinesis) and green (Actinidia deliciosa) kiwifruit by solution NMR spectroscopy. The chemical shift data confirm the characteristic Bet v 1 fold for both proteins, consisting of a seven-stranded antiparallel β-sheet interrupted by two short α-helices, along with a long C-terminal α-helix. Our data provide the basis for determining the three-dimensional solution structures of these proteins and characterizing their immunological cross-reactivity on a structural basis. PubMed: 34106433DOI: 10.1002/prot.20449 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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