3C3V

Crystal structure of peanut major allergen ara h 3

3C3V の概要

• エントリーDOI: 10.2210/pdb3c3v/pdb
• 分子名称: Arachin Arah3 isoform, SODIUM ION (3 entities in total)
• 機能のキーワード: peanut allergen, allergy, ara h 3, glycinin, allergen
• 由来する生物種: Arachis hypogaea (Peanut)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58577.71

構造登録者

Jin, T.,Zhang, Y. (登録日: 2008-01-28, 公開日: 2009-02-24, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.73 Å)