1. Dimerization of lipocalin allergens
- Author
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Marja Rytkönen-Nissinen, Janne Jänis, Merja Niemi, Ilja Miettinen, Tuomas Virtanen, and Juha Rouvinen
- Subjects
Intoxicative inhalant ,Models, Molecular ,Protein Conformation ,Dimer ,Lipocalin ,medicine.disease_cause ,Article ,Mass Spectrometry ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Allergen ,Protein structure ,medicine ,030304 developmental biology ,0303 health sciences ,Multidisciplinary ,integumentary system ,Chemistry ,Allergens ,Protein multimerization ,humanities ,Lipocalins ,3. Good health ,Animal allergens ,Biochemistry ,Protein Multimerization ,030217 neurology & neurosurgery - Abstract
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.
- Published
- 2015