AI Article Synopsis
- Fatty-acid binding proteins (FABPs) are key proteins that help transport and manage lipophilic molecules within cells, influencing metabolic and inflammatory processes.
- Human intestinal FABP (hIFABP) and rat intestinal FABP (rIFABP) exhibit variations in their binding affinities for certain ligands despite their similar structures.
- To investigate this difference, researchers have successfully crystallized hIFABP and rIFABP with a specific fluorescent fatty-acid analogue to study their structural interactions.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3034631 | PMC |
| http://dx.doi.org/10.1107/S1744309110051481 | DOI Listing |
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