Abstract
Fatty-acid binding proteins (FABPs) are abundantly expressed proteins that bind a range of lipophilic molecules. They have been implicated in the import and intracellular distribution of their ligands and have been linked with metabolic and inflammatory responses in the cells in which they are expressed. Despite their high sequence identity, human intestinal FABP (hIFABP) and rat intestinal FABP (rIFABP) bind some ligands with different affinities. In order to address the structural basis of this differential binding, diffraction-quality crystals have been obtained of hIFABP and rIFABP in complex with the fluorescent fatty-acid analogue 11-(dansylamino)undecanoic acid.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray / methods
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Escherichia coli / genetics
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Fatty Acid-Binding Proteins / analysis
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Fatty Acid-Binding Proteins / genetics
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Fatty Acid-Binding Proteins / isolation & purification
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Fatty Acid-Binding Proteins / metabolism*
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Fatty Acids / metabolism*
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Humans
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Hydrophobic and Hydrophilic Interactions
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Intestinal Mucosa / metabolism
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Ligands
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Protein Binding / genetics
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Rats
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Sequence Homology, Amino Acid
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Synchrotrons
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Transformation, Bacterial
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X-Ray Diffraction
Substances
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Fatty Acid-Binding Proteins
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Fatty Acids
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Ligands
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undecanoic acid