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 W Parker, Christopher JH Porter, Martin J Scanlon
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | INT UNION CRYSTALLOGRAPHY | Published : 2011
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.
Awarded by Australian Research Council
We would like to thank Janet Newman at the Bio21-C<SUP>3</SUP> Facility for support and helpful discussions. This research was partly undertaken on the MX1 beamline at the Australian Synchrotron, Victoria, Australia. We thank Rachael Williamson and Trevor Huyton for their help with data collection during our visit to the Australian Synchrotron. This work was supported by a grant from the Australian Research Council (DP0664069, DP0987500). MWP is an Australian Research Council Federation Fellow and National Health and Medical Research Council Honorary Fellow.