5lqq | pdb_00005lqq

Structure of Autotaxin (ENPP2) with LM350

spinqualitylabelsall models 5lqq, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lqq is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 72P, BMA, CA, IOD, MAN, NA, NAG, ZN Activity: Alkylglycerophosphoethanolamine phosphodiesterase, with EC number 3.1.4.39 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Autotaxin (ATX) is a secreted enzyme responsible for the hydrolysis of lysophosphatidylcholine (LPC) to the bioactive lysophosphatidic acid (LPA) and choline. The ATX-LPA signalling pathway is implicated in cell survival, migration, and proliferation; thus, the inhibition of ATX is a recognized therapeutic target for a number of diseases including fibrotic diseases, cancer, and inflammation, amongst others. Many of the developed synthetic inhibitors for ATX have resembled the lipid chemotype of the native ligand; however, a small number of inhibitors have been described that deviate from this common scaffold. Herein, we report the structure-activity relationships (SAR) of a previously reported small molecule ATX inhibitor. We show through enzyme kinetics studies that analogues of this chemotype are noncompetitive inhibitors, and using a crystal structure with ATX we confirm the discrete binding mode. Structure-activity Relationships of Small Molecule Autotaxin Inhibitors with a Discrete Binding Mode.,Miller LM, Keune WJ, Castagna D, Young LC, Duffy EL, Potjewyd F, Salgado-Polo F, Engel Garcia P, Semaan D, Pritchard JM, Perrakis A, Macdonald SJ, Jamieson C, Watson AJ J Med Chem. 2016 Dec 16. PMID:27982588 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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