Structural highlights
Function
MPAP5_PHLPR
Publication Abstract from PubMed
This is the first study determining the three-dimensional structure of Phl p 5a which reveals a novel mechanism for high allergenic activity based on flexibly connected IgE-reactive domains which cross-link effector cell-bound IgE more efficiently than isolated rigid globular proteins. These findings may also form a basis for specific immunotherapy strategies.
Flexible IgE epitope-containing domains of Phl p 5 cause high allergenic activity.,Gobl C, Focke-Tejkl M, Najafi N, Schrank E, Madl T, Kosol S, Madritsch C, Dorofeeva Y, Flicker S, Thalhamer J, Valenta R, Zangger K, Tjandra N J Allergy Clin Immunol. 2017 Oct;140(4):1187-1191. doi: , 10.1016/j.jaci.2017.05.005. Epub 2017 May 19. PMID:28532654[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Göbl C, Focke-Tejkl M, Najafi N, Schrank E, Madl T, Kosol S, Madritsch C, Dorofeeva Y, Flicker S, Thalhamer J, Valenta R, Zangger K, Tjandra N. Flexible IgE epitope-containing domains of Phl p 5 cause high allergenic activity. J Allergy Clin Immunol. 2017 Oct;140(4):1187-1191. PMID:28532654 doi:10.1016/j.jaci.2017.05.005
