Structural and functional analysis of fatty acid-binding proteins
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.Citation
Storch J, McDermott L (2009) 'Structural and functional analysis of fatty acid-binding proteins', Journal of Lipid Research, 50 (), pp.S126-S131.Journal
Journal of Lipid ResearchPubMed ID
19017610Additional Links
http://www.jlr.org/content/50/Supplement/S126.longType
ArticleLanguage
enISSN
0022-2275ae974a485f413a2113503eed53cd6c53
10.1194/jlr.R800084-JLR200
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