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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Allergens / immunology*
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Antigens, Plant / chemistry*
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Antigens, Plant / immunology
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Antigens, Plant / isolation & purification
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Betula / immunology
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Cross Reactions*
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Epitopes / immunology
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Fagus / immunology*
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Humans
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Molecular Dynamics Simulation
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Nuclear Magnetic Resonance, Biomolecular
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Plant Proteins / chemistry*
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Plant Proteins / immunology
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Plant Proteins / isolation & purification
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Pollen / immunology
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / immunology
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Recombinant Proteins / isolation & purification
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Structure-Activity Relationship
Substances
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Allergens
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Antigens, Plant
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Epitopes
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Plant Proteins
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Recombinant Proteins