6V8H

Crystal structure of Ara h 8.0201

6V8H の概要

• エントリーDOI: 10.2210/pdb6v8h/pdb
• 分子名称: Ara h 8 allergen isoform, SULFATE ION (3 entities in total)
• 機能のキーワード: peanut, allergen, pr-10
• 由来する生物種: Arachis hypogaea (Peanut)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 131651.86

構造登録者

Offermann, L.R.,Pote, S.,Hurlburt, B.K.,McBride, J.K.,Chruszcz, M. (登録日: 2019-12-11, 公開日: 2020-12-16, 最終更新日: 2025-12-03)

主引用文献

O'Malley, A.,Offermann, L.R.,Khatri, K.,Linn, C.,Pote, S.,McBride, J.K.,Perdue, M.L.,Hurlburt, B.K.,Maleki, S.J.,Mias, G.I.,Chruszcz, M.
Structural analysis of 8-anilino-1-naphthalene sulfonate (ANS) binding to the PR-10 allergen Ara h 8.
Biochem.Biophys.Res.Commun., 793:153013-153013, 2025

PubMed Abstract: We previously determined crystal structures of peanut allergen Ara h 8.0101 in the apo form as well as in complex with model ligands. These structures illustrated the varied ligand binding capabilities of PR-10s and Ara h 8's structural similarity to the major birch allergen Bet v 1. Here, we expanded on those structural studies with structures of Ara h 8.0101 and Ara h 8.0201 in complex with 8-anilino-1-naphthalene sulfonate (ANS), as well as the apo form of Ara h 8.0201. Structural studies revealed that both proteins may bind more than one ANS molecule. We also examined the impact of ANS on the ligand binding cavities of Ara h 8.0101 and Ara h 8.0201 with fluorescence assays and compared the results to prototypic PR-10 Bet v 1.0101. Moreover, as ANS is often used in fluorescence-based ligand binding assays, we analyzed structures from the PDB and provided a summary on experimentally determined ANS binding sites. These analyses show that ANS is useful for investigation of ligand binding sites, but it may also participate in non-specific reactions on nonpolar surfaces of proteins.

PubMed: 41274249
DOI: 10.1016/j.bbrc.2025.153013

実験手法

X-RAY DIFFRACTION (2.31 Å)