4azq

Murine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid 2-arachidonoylglycerol

spinqualitylabelsall models 4azq, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4azq is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: CL, G2A Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FABP5_MOUSE High specificity for fatty acids. Highest affinity for C18 chain length (By similarity). Publication Abstract from PubMed 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. Crystallographic study of FABP5 as an intracellular endocannabinoid transporter.,Sanson B, Wang T, Sun J, Wang L, Kaczocha M, Ojima I, Deutsch D, Li H Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):290-8. doi:, 10.1107/S1399004713026795. Epub 2014 Jan 29. PMID:24531463 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fatty acid-binding protein 3D structures

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