Dimerization of lipocalin allergens

Lipocalins are one of the most important groups of inhalant animal allergens. The analysis of structural features of these proteins is important to get insights into their allergenicity. We have determined two different dimeric crystal structures for bovine dander lipocalin Bos d 2, which was earlie...

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Veröffentlicht in:Scientific reports 2015-09, Vol.5 (1), p.13841-13841, Article 13841
Hauptverfasser: Niemi, Merja H., Rytkönen-Nissinen, Marja, Miettinen, Ilja, Jänis, Janne, Virtanen, Tuomas, Rouvinen, Juha
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Sprache:eng
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Zusammenfassung:Lipocalins are one of the most important groups of inhalant animal allergens. The analysis of structural features of these proteins is important to get insights into their allergenicity. We have determined two different dimeric crystal structures for bovine dander lipocalin Bos d 2, which was earlier described as a monomeric allergen. The crystal structure analysis of all other determined lipocalin allergens also revealed oligomeric structures which broadly utilize inherent structural features of the β-sheet in dimer formation. According to the moderate size of monomer-monomer interfaces, most of these dimers would be transient in solution. Native mass spectrometry was employed to characterize quantitatively transient dimerization of two lipocalin allergens, Bos d 2 and Bos d 5, in solution.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep13841