6ALK

NMR solution structure of the major beech pollen allergen Fag s 1

Summary for 6ALK

• Entry DOI: 10.2210/pdb6alk/pdb
• NMR Information: BMRB: 25590
• Descriptor: Fag s 1 pollen allergen (1 entity in total)
• Functional Keywords: allergen, ligand binding, conformational diversity
• Biological source: Fagus sylvatica (Beechnut)
• Total number of polymer chains: 1
• Total formula weight: 17250.39

Authors

Moraes, A.H.,Asam, A.,Almeida, F.C.L.,Wallner, M.,Ferreira, F.,Valente, A.P. (deposition date: 2017-08-08, release date: 2018-08-08, Last modification date: 2024-05-15)

Primary citation

Moraes, A.H.,Asam, C.,Almeida, F.C.L.,Wallner, M.,Ferreira, F.,Valente, A.P.
Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1.
Sci Rep, 8:10512-10512, 2018

PubMed 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 α-helices and seven β-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.

PubMed: 30002383
DOI: 10.1038/s41598-018-28358-1

Experimental method

SOLUTION NMR