ArticlePloS one2019
Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Structure and regulation of violaxanthin de-epoxidase, a key enzyme in the photoprotection of photosynthesis.Plant physiology · 2026Review
- Major Cat Allergen Fel d 4: Structure and Identification of a Cross-Reactive IgE-Epitope-Containing Area.Allergy · 2026Article
- A systematic review of allergen cross-reactivity: Translating basic concepts into clinical relevance.The journal of allergy and clinical immunology. Global · 2024Review
- Modern Concept of Molecular Diagnostics of Allergy to Dogs.Bulletin of experimental biology and medicine · 2023Review
- Component-Resolved Diagnosis Based on a Recombinant Variant of Mus m 1 Lipocalin Allergen.International journal of molecular sciences · 2023Article
- Mammalian derived lipocalin and secretoglobin respiratory allergens strongly bind ligands with potentially immune modulating properties.Frontiers in allergy · 2022Article
- Allergens and their associated small molecule ligands-their dual role in sensitization.Allergy · 2021Review
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Authors and funding
5 authors.
Funding
Abstract
Lipocalins represent the most important protein family of the mammalian respiratory allergens. Four of the seven named dog allergens are lipocalins: Can f 1, Can f 2, Can f 4, and Can f 6. We present the structure of Can f 6 along with data on the biophysical and biological activity of this protein in comparison with other animal lipocalins. The Can f 6 structure displays the classic lipocalin calyx-shaped ligand binding cavity within a central β-barrel similar to other lipocalins. Despite low sequence identity between the different dog lipocalin proteins, there is a high degree of structural similarity. On the other hand, Can f 6 has a similar primary sequence to cat, horse, mouse lipocalins as well as a structure that may underlie their cross reactivity. Interestingly, the entrance to the ligand binding pocket is capped by a His instead of the usually seen Tyr that may help select its natural ligand binding partner. Our highly pure recombinant Can f 6 is able to bind to human IgE (hIgE) demonstrating biological antigenicity.
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