%0 Journal Article
%A Stemeseder, Teresa
%A Freier, Regina
%A Wildner, Sabrina
%A Fuchs, Julian E
%A Briza, Peter
%A Lang, Roland
%A Batanero, Eva
%A Lidholm, Jonas
%A Liedl, Klaus R
%A Campo, Paloma
%A Hawranek, Thomas
%A Villalba, Mayte
%A Brandstetter, Hans
%A Ferreira, Fatima
%A Gadermaier, Gabriele
%T Crystal structure of Pla l 1 reveals both structural similarity and allergenic divergence within the Ole e 1-like protein family.
%D 2016
%U http://hdl.handle.net/10668/10675
%X Knowledge of structural and immunological features of allergens is important for understanding IgE sensitization and disease-eliciting mechanisms of allergenic molecules. Despite the fact that Ole e 1–like proteins are driving type I allergies within several pollen sources [1,2], there is currently no information regarding their tertiary structure. Ole e 1–like proteins are characterized by three conserved disulfide bonds and the [EQT]-G-X-V-Y-C-D-[TNP]-C-R consensus pattern, while their biological function remains unknown. To date, 14 allergenic members of this protein family, all originating from pollen, have been reported (www.allergen.org). These proteins exhibit varying degrees of sequence identity, typically high among Oleaceae species (>82%) but medium/low between botanically distant plants (25% to 60%).
%K Molecular Conformation
%K Plant Proteins
%K Structure-Activity Relationship
%~