| Crystal structure of peanut (Arachis hypogaea) allergen Ara h 5. | |
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MedLine Citation:
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PMID: 23350842 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Profilins from numerous species are known to be allergens, including food allergens, such as peanut (Arachis hypogaea) allergen Ara h 5, and pollen allergens, such as birch allergen Bet v 2. Patients with pollen allergy can also cross-react to peanut. Structural characterization of allergens will allow a better understanding of the allergenicity of food allergens and their cross-reactivities. The three-dimensional structures of most known food allergens remain to be elucidated. Here, we report the first crystallographic study of a food allergen in the profilin family. The structure of peanut allergen Ara h 5 was determined and the resolution of the final refined structure was 1.1 angstrom. Structure alignment revealed that Ara h 5 is more similar to Bet v 2 than to Hev b 8 although sequence alignment suggested that Ara h 5 is more closely related to Hev b 8 than to Bet v 2, indicating that homology model-based prediction of IgE epitopes needs to be interpreted with caution. |
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Authors:
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Yang Wang; Tong-Jen Fu; Andrew Howard; Mahendra H Kothary; Tara H McHugh; Yu-Zhu Zhang |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-25 |
Journal Detail:
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Title: Journal of agricultural and food chemistry Volume: - ISSN: 1520-5118 ISO Abbreviation: J. Agric. Food Chem. Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-1-28 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0374755 Medline TA: J Agric Food Chem Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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