6y5m

Crystal structure of mouse Autotaxin in complex with compound 1a

spinqualitylabelsall models 6y5m, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.011Å Ligands: BMA, CL, MAN, NA, NAG, O9W, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed A series of inhibitors of Autotaxin (ATX) have been developed from a high throughput screening hit, 1a, which shows an alternative binding mode to known catalytic site inhibitors. Selectivity over the hERG channel and microsomal clearance were dependent on the lipophilicity of the compounds, and this was optimised by reduction of clogD whilst maintaining high affinity ATX inhibition. Compound 15a shows good oral exposure, and concentration dependent inhibition of formation of LPA in vivo, as shown in pharmacokinetic-pharmacodynamic (PK/PD) experiments. Development of autotaxin inhibitors: A series of tetrazole cinnamides.,Thomson CG, Le Grand D, Dowling M, Beattie D, Elphick L, Faller M, Freeman M, Hardaker E, Head V, Hemmig R, Hill J, Lister A, Pascoe D, Rieffel S, Shrestha B, Steward O, Zink F Bioorg Med Chem Lett. 2020 Nov 4:127663. doi: 10.1016/j.bmcl.2020.127663. PMID:33160025 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ectonucleotide pyrophosphatase/phosphodiesterase 3D structures

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