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Publication Abstract from PubMed

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 beta-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.

Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6.,Clayton GM, White J, Lee S, Kappler JW, Chan SK PLoS One. 2019 Sep 16;14(9):e0213052. doi: 10.1371/journal.pone.0213052. , eCollection 2019. PMID:31525203^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.