5XND
Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel
Summary for 5XND
| Entry DOI | 10.2210/pdb5xnd/pdb |
| NMR Information | BMRB: 36086 |
| Descriptor | Parvalbumin beta, CALCIUM ION (2 entities in total) |
| Functional Keywords | structure from cyana 2.1, metal binding protein |
| Biological source | Scomber japonicus (Chub mackerel) |
| Total number of polymer chains | 1 |
| Total formula weight | 12053.74 |
| Authors | Kumeta, H.,Nakayama, H.,Ogura, K. (deposition date: 2017-05-22, release date: 2017-12-27, Last modification date: 2024-05-15) |
| Primary citation | Kumeta, H.,Nakayama, H.,Ogura, K. Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel Sci Rep, 7:17160-17160, 2017 Cited by PubMed Abstract: Although fish is an important part of the human diet, it is also a common source of food allergy. The major allergen in fish is parvalbumin, a well-conserved Ca-binding protein found in the white muscle of many fish species. Here, we studied the solution structure of the parvalbumin Sco j 1, derived from the Pacific mackerel, using nuclear magnetic resonance spectroscopy. We mapped the IgE-binding epitope proposed in a recent study onto the present structure. Interestingly, three of four residues, which were elucidated as key residues of the IgE-binding epitope, were exposed to solvent, whereas one residue faced the inside of the molecule. We expect that this solution structure can be used in future studies attempting to analyze the various IgE-binding modes of these allergens. PubMed: 29215073DOI: 10.1038/s41598-017-17281-6 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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