5hz5

FABP5 in complex with 6-Chloro-4-phenyl-2-piperidin-1-yl-3-(1H-tetrazol-5-yl)-quinoline

spinqualitylabelsall models 5hz5, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hz5 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 1.4Å Ligands: 65X, DMS, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FABP5_HUMAN High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation. 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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