Abstract
A D1 Fab fragment containing the allergen-binding variable domains of the IgE antibody was characterized by ESI FT-ICR mass spectrometry and crystallized with bovine beta-lactoglobulin (BLG) using the hanging-drop vapour-diffusion method at 293 K. X-ray data suitable for structure determination were collected to 2.8 A resolution using synchrotron radiation. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.0, b = 100.6, c = 168.1 A. The three-dimensional structure of the D1 Fab fragment-BLG complex will provide the first insight into IgE antibody-allergen interactions at the molecular level.
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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Amino Acid Sequence
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Animals
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Cattle
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Child
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Crystallography, X-Ray
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Food Hypersensitivity / immunology
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Humans
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Hypersensitivity / immunology
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Immunoglobulin E / chemistry*
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Immunoglobulin Fab Fragments / chemistry*
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Immunoglobulin Fab Fragments / isolation & purification
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Immunoglobulin Heavy Chains / chemistry
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Immunoglobulin Light Chains / chemistry
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Lactoglobulins / chemistry*
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Lactoglobulins / immunology*
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Lymphocytes / immunology
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Molecular Sequence Data
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Spectrum Analysis
Substances
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Allergens
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Immunoglobulin Fab Fragments
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Immunoglobulin Heavy Chains
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Immunoglobulin Light Chains
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Lactoglobulins
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Immunoglobulin E