4b10 | pdb_00004b10

Plasmodium vivax N-myristoyltransferase with a non-hydrolysable co- factor

spinqualitylabelsall models 4b10, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b10 is a 3 chain structure with sequence from Haemamoeba vivax. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, DMS, MG, NHW, SO4 Related: 4a95, 4b11, 4b12, 4b13, 4b14 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 Design of inhibitors for N-myristoyltransferase (NMT), an enzyme responsible for protein trafficking in Plasmodium falciparum , the most lethal species of parasites that cause malaria, is described. Chemistry-driven optimization of compound 1 from a focused NMT inhibitor library led to the identification of two early lead compounds 4 and 25, which showed good enzyme and cellular potency and excellent selectivity over human NMT. These molecules provide a valuable starting point for further development. Design and Synthesis of Inhibitors of Plasmodium falciparum N-Myristoyltransferase, A Promising Target for Antimalarial Drug Discovery.,Yu Z, Brannigan JA, Moss DK, Brzozowski AM, Wilkinson AJ, Holder AA, Tate EW, Leatherbarrow RJ J Med Chem. 2012 Oct 15. PMID:23035716 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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