9BB8

Crystal structure of human alpha parvalbumin

9BB8 の概要

• エントリーDOI: 10.2210/pdb9bb8/pdb
• 分子名称: Parvalbumin alpha, CALCIUM ION (3 entities in total)
• 機能のキーワード: parvalbumin, calcium binding protein, metal binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13895.76

構造登録者

O'Malley, A.,Chruszcz, M. (登録日: 2024-04-05, 公開日: 2024-12-04, 最終更新日: 2025-05-21)

主引用文献

O'Malley, A.,Ray, J.M.,Kitlas, P.,Ruethers, T.,Kapingidza, A.B.,Cierpicki, T.,Lopata, A.,Kowal, K.,Chruszcz, M.
Comparative studies of seafood and reptile alpha- and beta-parvalbumins.
Protein Sci., 33:e5226-e5226, 2024

PubMed Abstract: Small calcium-binding proteins such as parvalbumins (PVs) are major seafood and fish allergens. However, the impact of structural changes on their capacity to bind IgE has not been studied in detail. Therefore, fish and reptilian PVs, as well as human α-PV, were selected for biochemical, structural, and IgE binding studies. Likely due to their high solubility, crystallization proved difficult, so additional techniques were used to promote crystallization of the proteins. Novel crystal structures were determined for human PV, cod allergen Gad m 1.0201, saltwater crocodile allergen Cro p 1.0101, and the α-PV from thornback ray. β-PVs are considered the major fish allergens, while α-PVs are rarely categorized as allergens. To explain these differences, the results of structural and IgE binding studies were combined. This approach allowed us to provide new insight into IgE binding epitopes present on PVs, focusing on cross-reactivity among the selected α- and β-PVs. In addition, we have shown that these proteins display remarkable thermal stability across a range of pH conditions, which is relevant in the case of food allergens and food processing. Moreover, it is shown that the presence of calcium cations is critical for stability of the studied PVs via their protein folding, which has an impact on the formation of IgE binding epitopes. These studies shows the stability of fish and reptile PV allergens, and it allows for further evaluation of their IgE cross-reactivity.

PubMed: 39584689
DOI: 10.1002/pro.5226

実験手法

X-RAY DIFFRACTION (2.722 Å)