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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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Autores principales: Niemi, Merja H., Rytkönen-Nissinen, Marja, Miettinen, Ilja, Jänis, Janne, Virtanen, Tuomas, Rouvinen, Juha
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4561914/
https://www.ncbi.nlm.nih.gov/pubmed/26346541
http://dx.doi.org/10.1038/srep13841
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author Niemi, Merja H.
Rytkönen-Nissinen, Marja
Miettinen, Ilja
Jänis, Janne
Virtanen, Tuomas
Rouvinen, Juha
author_facet Niemi, Merja H.
Rytkönen-Nissinen, Marja
Miettinen, Ilja
Jänis, Janne
Virtanen, Tuomas
Rouvinen, Juha
author_sort Niemi, Merja H.
collection PubMed
description 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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spelling pubmed-45619142015-09-15 Dimerization of lipocalin allergens Niemi, Merja H. Rytkönen-Nissinen, Marja Miettinen, Ilja Jänis, Janne Virtanen, Tuomas Rouvinen, Juha Sci Rep Article 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. Nature Publishing Group 2015-09-08 /pmc/articles/PMC4561914/ /pubmed/26346541 http://dx.doi.org/10.1038/srep13841 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Niemi, Merja H.
Rytkönen-Nissinen, Marja
Miettinen, Ilja
Jänis, Janne
Virtanen, Tuomas
Rouvinen, Juha
Dimerization of lipocalin allergens
title Dimerization of lipocalin allergens
title_full Dimerization of lipocalin allergens
title_fullStr Dimerization of lipocalin allergens
title_full_unstemmed Dimerization of lipocalin allergens
title_short Dimerization of lipocalin allergens
title_sort dimerization of lipocalin allergens
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4561914/
https://www.ncbi.nlm.nih.gov/pubmed/26346541
http://dx.doi.org/10.1038/srep13841
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