Abstract
Odorant-binding proteins (OBPs) are small abundant soluble proteins belonging to the lipocalin superfamily, which are thought to carry hydrophobic odorants through aqueous mucus towards olfactory receptors. Human variant hOBP-2A has been demonstrated to bind numerous odorants of different chemical classes with a higher affinity for aldehydes and fatty acids. Three lysyl residues of the binding pocket (Lys62, Lys82 and Lys112) have been suggested as candidates for playing such a role. Here, using site-directed mutagenesis and fluorescent probe displacements, we show that Lys112 is the major determinant for governing hOBP-2A specificity towards aldehydes and small carboxylic acids.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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1-Naphthylamine / analogs & derivatives
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Aldehydes / metabolism*
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Amino Acid Sequence
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Animals
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism*
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Dansyl Compounds
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Fatty Acids
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Fluorescent Dyes
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Humans
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Ligands
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Lipocalins
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Lysine / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis
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Mutation / genetics
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Palmitic Acid / metabolism
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Protein Binding
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Recombinant Proteins / metabolism
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Sequence Homology
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Substrate Specificity
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Titrimetry
Substances
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Aldehydes
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Carrier Proteins
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Dansyl Compounds
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Fatty Acids
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Fluorescent Dyes
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Ligands
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Lipocalins
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OBP2A protein, human
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Recombinant Proteins
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Palmitic Acid
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11-(dansylamino)undecanoic acid
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N-phenyl-1-naphthylamine
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1-Naphthylamine
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undecanal
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Lysine