4MA6

Crystal structure of Ara h 8 with Epicatechin bound

Summary for 4MA6

• Entry DOI: 10.2210/pdb4ma6/pdb
• Related: 4M9B 4M9W 4MAP
• Descriptor: Ara h 8 allergen, SODIUM ION, (2R,3R)-2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-chromene-3,5,7-triol, ... (4 entities in total)
• Functional Keywords: bet v 1 like, small molecule carrier, plant protein
• Biological source: Arachis hypogaea (goober,ground-nut)
• Total number of polymer chains: 2
• Total formula weight: 34282.67

Authors

Offermann, L.R.,Hurlburt, B.K.,Majorek, K.A.,McBride, J.K.,Maleki, S.J.,Chruszcz, M. (deposition date: 2013-08-15, release date: 2013-11-27, Last modification date: 2023-09-20)

Primary citation

Hurlburt, B.K.,Offermann, L.R.,McBride, J.K.,Majorek, K.A.,Maleki, S.J.,Chruszcz, M.
Structure and Function of the Peanut Panallergen Ara h 8.
J.Biol.Chem., 288:36890-36901, 2013

PubMed Abstract: The incidence of peanut allergy continues to rise in the United States and Europe. Whereas exposure to the major allergens Ara h 1, 2, 3, and 6 can cause fatal anaphylaxis, exposure to the minor allergens usually does not. Ara h 8 is a minor allergen. Importantly, it is the minor food allergens that are thought to be responsible for oral allergy syndrome (OAS), in which sensitization to airborne allergens causes a Type 2 allergic reaction to ingested foods. Furthermore, it is believed that similar protein structure rather than a similar linear sequence is the cause of OAS. Bet v 1 from birch pollen is a common sensitizing agent, and OAS results when patients consume certain fruits, vegetables, tree nuts, and peanuts. Here, we report the three-dimensional structure of Ara h 8, a Bet v 1 homolog. The overall fold is very similar to that of Bet v 1, Api g 1 (celery), Gly m 4 (soy), and Pru av 1 (cherry). Ara h 8 binds the isoflavones quercetin and apigenin as well as resveratrol avidly.

PubMed: 24253038
DOI: 10.1074/jbc.M113.517797

Experimental method

X-RAY DIFFRACTION (2 Å)