Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1.

ABSTRACT: Fag s 1 is a member of the Pathogen Related protein family 10 (PR-10) and can elicit cross-reaction with IgE antibodies produced against the birch pollen allergen Bet v 1. The Nuclear Magnetic Resonance (NMR) structure of Fag s 1 is presented along with its dynamic properties. It shares 66% identity with Bet v 1 and exhibits the expected three ?-helices and seven ?-sheets arranged as a semi-beta barrel and exposing the residues mapped as the Bet v 1 IgE epitope. The structural dynamics of Fag s 1 were monitored on the fast and intermediate timescales, using relaxation rates. The complex dynamics of Fag s 1 are closely related to the internal cavity, and they modulate IgE and ligand binding.

SUBMITTER: Moraes AH 

PROVIDER: S-EPMC6043577 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature