Dimerization of lipocalin allergens

Scientific Reports
Merja NiemiJuha Rouvinen

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.

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Citations

Oct 30, 2016·Current Opinion in Immunology·Isabella Pali-Schöll, Erika Jensen-Jarolim
Aug 29, 2018·Proceedings of the National Academy of Sciences of the United States of America·Alkistis N MitropoulouBrian J Sutton
Jun 24, 2020·Nature Immunology·Ursula SmoleMarsha Wills-Karp
Dec 17, 2019·Biophysical Chemistry·Homero Gómez-VelascoEnrique García-Hernández
Sep 5, 2021·Biological Reviews of the Cambridge Philosophical Society·Paolo Pelosi, Wolfgang Knoll

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Methods Mentioned

BETA
isothermal titration calorimetry
size-exclusion chromatography
X-ray
PISA

Software Mentioned

AUC
XSCALE
PHENIX
PDBePISA
PISA
Phaser
PYMOL
CCP4 suite
XDS
Procheck

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