Preparation, crystallization and preliminary X-ray diffraction analysis of two intestinal fatty-acid binding proteins in the presence of 11-(dansylamino)undecanoic acid

Aisha Laguerre, Jerome Wielens, Michael Parker, Christopher Porter, Martin Scanlon

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)291 - 295
Number of pages5
Journal Acta Crystallographica Section F: Structural Biology Communications
Volume67
Issue number2
DOIs
Publication statusPublished - 2011

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