5hz8

FABP4_3 in complex with 6,8-Dichloro-4-phenyl-2-piperidin-1-yl-quinoline-3-carboxylic acid

spinqualitylabelsall models 5hz8, resolution 1.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hz8 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.12Å Ligands: 65Z, DMS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FABP4_HUMAN Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). Publication Abstract from PubMed Dual inhibition of fatty acid binding proteins 4 and 5 (FABP4 and FABP5) is expected to provide beneficial effects on a number of metabolic parameters such as insulin sensitivity and blood glucose levels and should protect against atherosclerosis. Starting from a FABP4 selective focused screening hit, biostructure information was used to modulate the selectivity profile in the desired way and to design potent dual FABP4/5 inhibitors with good selectivity against FABP3. With very good pharmacokinetic properties and no major safety alerts, compound 12 was identified as a suitable tool compound for further in vivo investigations. Design and synthesis of selective, dual fatty acid binding protein 4 and 5 inhibitors.,Kuhne H, Obst-Sander U, Kuhn B, Conte A, Ceccarelli SM, Neidhart W, Rudolph MG, Ottaviani G, Gasser R, So SS, Li S, Zhang X, Gao L, Myers M Bioorg Med Chem Lett. 2016 Oct 15;26(20):5092-5097. doi:, 10.1016/j.bmcl.2016.08.071. Epub 2016 Aug 22. PMID:27658368 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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