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4XUW

Structure of the hazelnut allergen, Cor a 8

Summary for 4XUW
Entry DOI10.2210/pdb4xuw/pdb
DescriptorNon-specific lipid-transfer protein, PHOSPHATE ION (3 entities in total)
Functional Keywordsallergen, plant protein
Biological sourceCorylus avellana (European hazel)
Total number of polymer chains2
Total formula weight19068.99
Authors
Offermann, L.R.,Perdue, M.L.,Bublin, M.,Pfeifer, S.,Dubiela, P.,Hoffmann-Sommergruber, K.,Chruszcz, M. (deposition date: 2015-01-26, release date: 2015-10-14, Last modification date: 2024-10-16)
Primary citationOffermann, L.R.,Bublin, M.,Perdue, M.L.,Pfeifer, S.,Dubiela, P.,Borowski, T.,Chruszcz, M.,Hoffmann-Sommergruber, K.
Structural and Functional Characterization of the Hazelnut Allergen Cor a 8.
J.Agric.Food Chem., 63:9150-9158, 2015
Cited by
PubMed Abstract: Nonspecific lipid transfer proteins (nsLTPs) are basic proteins, stabilized by four disulfide bonds, and are expressed throughout the plant kingdom. These proteins are also known as important allergens in fruits and tree nuts. In this study, the nsLTP from hazelnuts, Cor a 8, was purified and its crystal structure determined. The protein is stable at low pH and refolds after thermal denaturation. Molecular dynamics simulations were used to provide an insight into conformational changes of Cor a 8 upon ligand binding. When known epitope areas from Pru p 3 were compared to those of Cor a 8, differences were obvious, which may contribute to limited cross-reactivity between peach and hazelnut allergens. Differences in epitope regions may contribute to limited cross-reactivity between Cor a 8 and nsLTPs from other plant sources. The structure of Cor a 8 represents the first resolved structure of a hazelnut allergen.
PubMed: 26417906
DOI: 10.1021/acs.jafc.5b03534
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.1 Å)
Structure validation

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