8V5Y

Crystal structure of Tyr p 36.0101 in complex with a poly(L-proline) peptide

8V5Y の概要

• エントリーDOI: 10.2210/pdb8v5y/pdb
• 分子名称: Profilin, poly(L-proline) peptide, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: mite profilin, storage mite, allergy, allergen, poly(l-proline) peptide
• 由来する生物種: Tyrophagus putrescentiae; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 34748.78

構造登録者

O'Malley, A.,Chruszcz, M. (登録日: 2023-12-01, 公開日: 2024-05-08, 最終更新日: 2024-06-19)

主引用文献

O'Malley, A.,Sankaran, S.,Carriuolo, A.,Khatri, K.,Kowal, K.,Chruszcz, M.
Structural homology of mite profilins to plant profilins is not indicative of allergic cross-reactivity.
Biol.Chem., 405:367-381, 2024

PubMed Abstract: Structural and allergenic characterization of mite profilins has not been previously pursued to a similar extent as plant profilins. Here, we describe structures of profilins originating from (registered allergen Tyr p 36.0101) and (here termed Der p profilin), which are the first structures of profilins from Arachnida. Additionally, the thermal stabilities of mite and plant profilins are compared, suggesting that the high number of cysteine residues in mite profilins may play a role in their increased stability. We also examine the cross-reactivity of plant and mite profilins as well as investigate the relevance of these profilins in mite inhalant allergy. Despite their high structural similarity to other profilins, mite profilins have low sequence identity with plant and human profilins. Subsequently, these mite profilins most likely do not display cross-reactivity with plant profilins. At the same time the profilins have highly conserved poly(l-proline) and actin binding sites.

PubMed: 38662449
DOI: 10.1515/hsz-2023-0366

実験手法

X-RAY DIFFRACTION (2.059 Å)