3C3V

Crystal structure of peanut major allergen ara h 3

Summary for 3C3V

• Entry DOI: 10.2210/pdb3c3v/pdb
• Descriptor: Arachin Arah3 isoform, SODIUM ION (3 entities in total)
• Functional Keywords: peanut allergen, allergy, ara h 3, glycinin, allergen
• Biological source: Arachis hypogaea (Peanut)
• Total number of polymer chains: 1
• Total formula weight: 58577.71

Authors

Jin, T.,Zhang, Y. (deposition date: 2008-01-28, release date: 2009-02-24, Last modification date: 2024-10-30)

Primary citation

Jin, T.,Guo, F.,Chen, Y.W.,Howard, A.,Zhang, Y.Z.
Crystal structure of Ara h 3, a major allergen in peanut.
Mol.Immunol., 46:1796-1804, 2009

PubMed Abstract: The prevalence of food allergy has increased dramatically in recent years. Tremendous research progress has been made in understanding the pathophysiological mechanisms of allergy and in identifying and characterizing food allergens. Peanut is a major food allergen source and Ara h 3 is a major peanut allergen. Using overlapping short peptides, several linear IgE-binding epitopes in Ara h 3 have been defined before. However, the structure of Ara h 3 of the native allergen is not clear and information on conformational epitopes is lacking. Structural characterization of allergens is required for understanding the allergenicity of food allergens and for the development of immunotherapeutic agents. Previously, we have reported the crystallization of Ara h 3 purified from raw peanut. Here we report the crystal structure of Ara h 3 at 1.73A resolution. Mapping of the previously defined linear epitopes on the crystal structure of Ara h 3 indicated that linear epitopes with more solvent exposure were those indicated by the literature to react with more patient sera. The structure of Ara h 3 may be used to assess the importance of conformational epitopes in further investigations.

PubMed: 19251323
DOI: 10.1016/j.molimm.2009.01.023

Experimental method

X-RAY DIFFRACTION (1.73 Å)