5hz9 | pdb_00005hz9

human FABP3 in complex with 6-Chloro-2-methyl-4-phenyl-quinoline-3-carboxylic acid

spinqualitylabelsall models 5hz9, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hz9 is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 5M8, CL, SO4 Gene: FABP3, FABP11, MDGI (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FABPH_HUMAN] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. 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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