Crystallographically mapped ligand binding differs in high and low IgE binding isoforms of birch pollen allergen bet v 1.

ABSTRACT: The ability of pathogenesis-related proteins of family 10 to bind a broad spectrum of ligands is considered to play a key role for their physiological and pathological functions. In particular, Bet v 1, an archetypical allergen from birch pollen, is described as a highly promiscuous ligand acceptor. However, the detailed recognition mechanisms, including specificity factors discriminating binding properties of naturally occurring Bet v 1 variants, are poorly understood. Here, we report crystal structures of Bet v 1 variants in complex with an array of ligands at a resolution of up to 1.2 Å. Residue 30 within the hydrophobic pocket not only discriminates in high and low IgE binding Bet v 1 isoforms but also induces a drastic change in the binding mode of the model ligand deoxycholate. Terna

SUBMITTER: Kofler S 

PROVIDER: S-EPMC3422537 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature