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Crystallographic Study of FABP5 as an Intracellular Endocannabinoid Transporter

Crystallographic Study of FABP5 as an Intracellular Endocannabinoid Transporter

Benoît Sanson, Tao Wang, Jing Sun, Liqun Wang, Martin Kaczocha, Iwao Ojima, Dale Deutsch, Huilin Li

Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):290-8.

PMID: 24531463

Abstract:

In addition to binding intracellular fatty acids, fatty-acid-binding proteins (FABPs) have recently been reported to also transport the endocannabinoids anandamide (AEA) and 2-arachidonoylglycerol (2-AG), arachidonic acid derivatives that function as neurotransmitters and mediate a diverse set of physiological and psychological processes. To understand how the endocannabinoids bind to FABPs, the crystal structures of FABP5 in complex with AEA, 2-AG and the inhibitor BMS-309403 were determined. These ligands are shown to interact primarily with the substrate-binding pocket via hydrophobic interactions as well as a common hydrogen bond to the Tyr131 residue. This work advances our understanding of FABP5-endocannabinoid interactions and may be useful for future efforts in the development of small-molecule inhibitors to raise endocannabinoid levels.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP300657038	BMS-309403		300657-03-8	Price

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