6V8S
Crystal structure of Ara h 8.0201
Summary for 6V8S
| Entry DOI | 10.2210/pdb6v8s/pdb |
| Descriptor | Ara h 8 allergen isoform, 8-ANILINO-1-NAPHTHALENE SULFONATE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | peanut, allergen, pr-10 |
| Biological source | Arachis hypogaea (Peanut) |
| Total number of polymer chains | 16 |
| Total formula weight | 293548.62 |
| Authors | Pote, S.,Offermann, L.R.,Hurlburt, B.K.,McBride, J.K.,Chruszcz, M. (deposition date: 2019-12-12, release date: 2020-12-16, 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 Cited by 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: 41274249DOI: 10.1016/j.bbrc.2025.153013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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