6AWR

Structure of PR 10 Allergen Ara h 8.01 in complex with ANS

Summary for 6AWR

• Entry DOI: 10.2210/pdb6awr/pdb
• Descriptor: Ara h 8 allergen, 8-ANILINO-1-NAPHTHALENE SULFONATE, SODIUM ION, ... (5 entities in total)
• Functional Keywords: plant protein, peanut, allergen, protein binding
• Biological source: Arachis hypogaea (Peanut)
• Total number of polymer chains: 2
• Total formula weight: 34806.21

Authors

Offermann, L.R.,McBride, J.,Hurlburt, B.K.,Maleki, S.J.,Pote, S.S.,Perdue, M.,Chruszcz, M. (deposition date: 2017-09-06, release date: 2018-09-12, Last modification date: 2025-12-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)