Abstract
A full characterization of the high-resolution NMR spectrum of the laminarihexaose is described and used for the determination of the binding epitope of the more complex but structurally related laminarin. These biophysical data extend the current knowledge of β-glucans/Dectin-1 interactions and suggest different biological mechanisms in close relation with the size of the saccharidic chain.
Copyright © 2011 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Carbohydrate Sequence
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Epitope Mapping
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Glucans
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Humans
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Immunologic Factors / chemistry*
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Immunologic Factors / metabolism
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Lectins, C-Type
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Macrophage-1 Antigen / chemistry
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Macrophage-1 Antigen / immunology
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Macrophage-1 Antigen / metabolism*
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Magnetic Resonance Spectroscopy / methods*
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Membrane Proteins / chemistry
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Membrane Proteins / immunology
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Membrane Proteins / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / immunology
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Nerve Tissue Proteins / metabolism*
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Oligosaccharides / chemistry*
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Oligosaccharides / metabolism
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Polysaccharides / chemistry*
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Polysaccharides / metabolism
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Protein Binding
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Recombinant Proteins / chemistry
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Recombinant Proteins / immunology
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Recombinant Proteins / metabolism*
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Structure-Activity Relationship
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beta-Glucans / chemistry*
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beta-Glucans / metabolism
Substances
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Glucans
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Immunologic Factors
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Lectins, C-Type
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Macrophage-1 Antigen
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Membrane Proteins
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Nerve Tissue Proteins
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Oligosaccharides
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Polysaccharides
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Recombinant Proteins
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beta-Glucans
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dectin 1
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laminarihexaose
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laminaran