Structural highlights
Function
[ALL2_BOVIN] Probable pheromone carrier.
Publication Abstract from PubMed
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 beta-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.
Dimerization of lipocalin allergens.,Niemi MH, Rytkonen-Nissinen M, Miettinen I, Janis J, Virtanen T, Rouvinen J Sci Rep. 2015 Sep 8;5:13841. doi: 10.1038/srep13841. PMID:26346541[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Niemi MH, Rytkonen-Nissinen M, Miettinen I, Janis J, Virtanen T, Rouvinen J. Dimerization of lipocalin allergens. Sci Rep. 2015 Sep 8;5:13841. doi: 10.1038/srep13841. PMID:26346541 doi:http://dx.doi.org/10.1038/srep13841
