5MMU
NMR solution structure of the major apple allergen Mal d 1
Summary for 5MMU
| Entry DOI | 10.2210/pdb5mmu/pdb |
| NMR Information | BMRB: 25968 |
| Descriptor | Major allergen Mal d 1 (1 entity in total) |
| Functional Keywords | pr-10 protein apple allergen, allergen |
| Biological source | Malus domestica (Apple) |
| Total number of polymer chains | 1 |
| Total formula weight | 17543.69 |
| Authors | Ahammer, L.,Grutsch, S.,Kamenik, A.S.,Liedl, K.R.,Tollinger, M. (deposition date: 2016-12-12, release date: 2017-02-15, Last modification date: 2024-05-15) |
| Primary citation | Ahammer, L.,Grutsch, S.,Kamenik, A.S.,Liedl, K.R.,Tollinger, M. Structure of the Major Apple Allergen Mal d 1. J. Agric. Food Chem., 65:1606-1612, 2017 Cited by PubMed Abstract: 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 β-sheet and three α-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. PubMed: 28161953DOI: 10.1021/acs.jafc.6b05752 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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