5g22 | pdb_00005g22

Plasmodium vivax N-myristoyltransferase in complex with a quinoline inhibitor (compound 26)

spinqualitylabelsall models 5g22, resolution 2.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g22 is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MG, NHW, SO4, YN4 Related: 5g1z, 5g20, 5g21 Activity: Glycylpeptide N-tetradecanoyltransferase, with EC number 2.3.1.97 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A5K1A2_PLAVS] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] Publication Abstract from PubMed The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT). Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.,Goncalves V, Brannigan JA, Laporte A, Bell AS, Roberts SM, Wilkinson AJ, Leatherbarrow RJ, Tate EW Medchemcomm. 2017 Jan 1;8(1):191-197. doi: 10.1039/c6md00531d. Epub 2016 Nov 11. PMID:28626547 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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