Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6
Autoři:
Gina M. Clayton aff001; Janice White aff001; Schuyler Lee aff001; John W. Kappler aff001; Sanny K. Chan aff001
Působiště autorů:
Department of Biomedical Research, National Jewish Health, Denver, Colorado, United States of America
aff001; Program in Structural Biology and Biochemistry, University of Colorado Denver School of Medicine, Aurora, Colorado, United States of America
aff002; Department of Biochemistry and Molecular Genetics, University of Colorado Denver School of Medicine, Aurora, Colorado, United States of America
aff003; Department of Immunology and Microbiology, University of Colorado Denver School of Medicine, Aurora, Colorado, United States of America
aff004; Department of Pediatrics, University of Colorado Denver School of Medicine, Aurora, Colorado, United States of America
aff005; Division of Pediatric Allergy-Immunology, National Jewish Health, Denver, Colorado, United States of America
aff006
Vyšlo v časopise:
PLoS ONE 14(9)
Kategorie:
Research Article
doi:
https://doi.org/10.1371/journal.pone.0213052
Souhrn
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.
Klíčová slova:
Physical sciences – Physics – Condensed matter physics – Solid state physics – Crystallography – Crystal structure – Biology and life sciences – Organisms – Eukaryota – Animals – Vertebrates – Amniotes – Mammals – Dogs – Cats – Allergies – Allergens – Molecular biology – Macromolecular structure analysis – Protein structure comparison – Biochemistry – Proteins – Protein structure – Post-translational modification – Phosphorylation – Glycobiology – Glycosylation – Medicine and health sciences – Clinical medicine – Clinical immunology – Immunology – Research and analysis methods – Crystallographic techniques – Crystal structure refinement
Zdroje
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