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J Lipid Res. 2009 Apr;50 Suppl:S126-31. doi: 10.1194/jlr.R800084-JLR200. Epub 2008 Nov 17.

Structural and functional analysis of fatty acid-binding proteins.

Author information

1
Department of Nutritional Sciences, Rutgers Center for Lipid Research, Rutgers University, New Brunswick, NJ 08901, USA. storch@aesop.rutgers.edu

Abstract

The mammalian FA-binding proteins (FABPs) bind long-chain FA with high affinity. The large number of FABP types is suggestive of distinct functions in specific tissues. Multiple experimental approaches have shown that individual FABPs possess both unique and overlapping functions, some of which are based on specific elements in the protein structure. Although FA binding affinities for all FABPs tend to correlate directly with FA hydrophobicity, structure-function studies indicate that subtle three-dimensional changes that occur upon ligand binding may promote specific protein-protein or protein-membrane interactions that ultimately determine the function of each FABP. The conformational changes are focused in the FABP helical/portal domain, a region that was identified by in vitro studies to be vital for the FA transport properties of the FABPs. Thus, the FABPs modulate intracellular lipid homeostasis by regulating FA transport in the nuclear and extra-nuclear compartments of the cell; in so doing, they also impact systemic energy homeostasis.

PMID:
19017610
PMCID:
PMC2674722
DOI:
10.1194/jlr.R800084-JLR200
[Indexed for MEDLINE]
Free PMC Article

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