5mmu

NMR solution structure of the major apple allergen Mal d 1

spinqualitylabelsall models 5mmu Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mmu is a 1 chain structure with sequence from Malus domestica. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MAL11_MALDO Publication Abstract from PubMed More than 70% of birch pollen-allergic patients develop allergic cross-reactions to the major allergen found in apple fruits (Malus domestica), the 17.5 kDa protein Mal d 1. Allergic reactions against this protein result from initial sensitization to the major allergen from birch pollen, Bet v 1. Immunologic cross-reactivity of Bet v 1-specific IgE antibodies with Mal d 1 after apple consumption can subsequently provoke severe oral allergic syndromes. This study presents the three-dimensional NMR solution structure of Mal d 1 (isoform Mal d 1.0101, initially cloned from 'Granny Smith' apples). This protein is composed of a seven-stranded antiparallel beta-sheet and three alpha-helices that form a large internal cavity, similar to Bet v 1 and other cross-reactive food allergens. The Mal d 1 structure provides the basis for elucidating the details of allergic cross-reactivity between birch pollen and apple allergens on a molecular level. Structure of the Major Apple Allergen Mal d 1.,Ahammer L, Grutsch S, Kamenik AS, Liedl KR, Tollinger M J Agric Food Chem. 2017 Mar 1;65(8):1606-1612. doi: 10.1021/acs.jafc.6b05752., Epub 2017 Feb 15. PMID:28161953 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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