Summary for 7U1I
| Entry DOI | 10.2210/pdb7u1i/pdb |
| Descriptor | Vicilin (2 entities in total) |
| Functional Keywords | pisum sativum, pis s 1, vicilin, seed storage protein, allergen |
| Biological source | Pisum sativum (pea) |
| Total number of polymer chains | 3 |
| Total formula weight | 146358.88 |
| Authors | Beavington, B.A.G.,Bakestani, I.D.,Robinson, K.A.,Loewen, M.C. (deposition date: 2022-02-21, release date: 2022-03-16, Last modification date: 2023-10-25) |
| Primary citation | Robinson, K.A.,St-Jacques, A.D.,Bakestani, I.D.,Beavington, B.A.G.,Loewen, M.C. Pea and lentil 7S globulin crystal structures with comparative immunoglobulin epitope mapping. Food Chem (Oxf), 5:100146-100146, 2022 Cited by PubMed Abstract: Legumes represent an affordable high protein, nutrient dense food source. However, the vast majority of legume crops contain proteins that are known allergens for susceptible individuals. These include proteins from the 7S globulin family, which comprise a vast majority of seed storage proteins. Here, the crystal structures of 7S globulins from L. (pea) and Medicus (lentil) are presented for the first time, including pea vicillin and convicilin, and lentil vicilin. All three structures maintain the expected 7S globulin fold, with trimeric quaternary structure and monomers comprised of β-barrel N- and C-modules. The potential impact of sequence differences on structure and packing in the different crystal space groups is noted, with potential relevance to packing upon seed deposition. Mapping on the obtained crystal structures highlights significant Ig epitope overlap between pea, lentil, peanut and soya bean and significant coverage of the entire seed storage protein, emphasizing the challenge in addressing food allergies. How recently developed biologicals might be refined to be more effective, or how these seed storage proteins might be modified to be less immuno-reactive remain challenges for the future. With legumes representing an affordable, high protein, nutrient dense food source, this work will enable important research in the context of global food security and human health on an ongoing basis. PubMed: 36573105DOI: 10.1016/j.fochms.2022.100146 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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