4C7H
Leismania major N-myristoyltransferase in complex with a peptidomimetic (-NH2) molecule
Summary for 4C7H
| Entry DOI | 10.2210/pdb4c7h/pdb |
| Related | 4C68 4C7I |
| Descriptor | GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, MAGNESIUM ION, N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide, ... (8 entities in total) |
| Functional Keywords | transferase, myristoylation |
| Biological source | LEISHMANIA MAJOR |
| Total number of polymer chains | 1 |
| Total formula weight | 50669.96 |
| Authors | Olaleye, T.O.,Brannigan, J.A.,Goncalves, V.,Roberts, S.M.,Leatherbarrow, R.J.,Wilkinson, A.J.,Tate, E.W. (deposition date: 2013-09-20, release date: 2014-09-24, Last modification date: 2024-05-08) |
| Primary citation | Olaleye, T.O.,Brannigan, J.A.,Roberts, S.M.,Leatherbarrow, R.J.,Wilkinson, A.J.,Tate, E.W. Peptidomimetic Inhibitors of N-Myristoyltransferase from Human Malaria and Leishmaniasis Parasites. Org.Biomol.Chem., 12:8132-, 2014 Cited by PubMed Abstract: N-Myristoyltransferase (NMT) has been shown to be essential in Leishmania and subsequently validated as a drug target in Plasmodium. Herein, we discuss the use of antifungal NMT inhibitors as a basis for inhibitor development resulting in the first sub-micromolar peptidomimetic inhibitors of Plasmodium and Leishmania NMTs. High-resolution structures of these inhibitors with Plasmodium and Leishmania NMTs permit a comparative analysis of binding modes, and provide the first crystal structure evidence for a ternary NMT-Coenzyme A/myristoylated peptide product complex. PubMed: 25230674DOI: 10.1039/C4OB01669F PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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