5XND

Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel

5XND の概要

• エントリーDOI: 10.2210/pdb5xnd/pdb
• NMR情報: BMRB: 36086
• 分子名称: Parvalbumin beta, CALCIUM ION (2 entities in total)
• 機能のキーワード: structure from cyana 2.1, metal binding protein
• 由来する生物種: Scomber japonicus (Chub mackerel)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12053.74

構造登録者

Kumeta, H.,Nakayama, H.,Ogura, K. (登録日: 2017-05-22, 公開日: 2017-12-27, 最終更新日: 2024-05-15)

主引用文献

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

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: 29215073
DOI: 10.1038/s41598-017-17281-6

実験手法

SOLUTION NMR