4ma6 | pdb_00004ma6

Crystal structure of Ara h 8 with Epicatechin bound

spinqualitylabelsall models 4ma6, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ma6 is a 2 chain structure with sequence from Arachis hypogaea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: 28E, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6VT83_ARAHY Publication Abstract from PubMed 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. Structure and Function of the Peanut Panallergen Ara h 8.,Hurlburt BK, Offermann LR, McBride JK, Majorek KA, Maleki SJ, Chruszcz M J Biol Chem. 2013 Dec 27;288(52):36890-901. doi: 10.1074/jbc.M113.517797. Epub, 2013 Nov 19. PMID:24253038 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA