5a27

Leishmania major N-myristoyltransferase in complex with a chlorophenyl 1,2,4-oxadiazole inhibitor.

spinqualitylabelsall models 5a27, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a27 is a 1 chain structure with sequence from Leishmania major. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.37Å Ligands: MG, MYA, TUT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4Q5S8_LEIMA Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity). Publication Abstract from PubMed N-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity. Discovery of high affinity inhibitors of -myristoyltransferase.,Rackham MD, Yu Z, Brannigan JA, Heal WP, Paape D, Barker KV, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW Medchemcomm. 2015 Oct 8;6(10):1761-1766. Epub 2015 Aug 19. PMID:26962429 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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