6lka

Crystal Structure of EV71-3C protease with a Novel Macrocyclic CompoundsCrystal Structure of EV71-3C protease with a Novel Macrocyclic Compounds

Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.033Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed We describe here the design, synthesis, and evaluation of a macrocyclic peptidomimetic as a potent agent targeting enterovirus A71 (EV71). The compound has a 15-membered macrocyclic ring in a defined conformation. Yamaguchi esterification reaction was used to close the 15-membered macrocycle instead of the typical Ru-catalyzed ring-closing olefin metathesis reaction. The crystallographic characterization of the complex between this compound and its target, 3C protease from EV71, validated the design and paved the way for the generation of a new series of anti-EV71 agents. Design, synthesis, and evaluation of a novel macrocyclic anti-EV71 agent.,Li P, Wu S, Xiao T, Li Y, Su Z, Wei W, Hao F, Hu G, Lin F, Chen X, Gu Z, Lin T, He H, Li J, Chen S Bioorg Med Chem. 2020 Jun 15;28(12):115551. doi: 10.1016/j.bmc.2020.115551. Epub , 2020 May 8. PMID:32503695 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proteinase 3D structures Virus protease 3D structures

spinqualitylabelsall models 6lka, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image