Structural highlights
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) 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.
Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites.,Olaleye TO, Brannigan JA, Roberts SM, Leatherbarrow RJ, Wilkinson AJ, Tate EW Org Biomol Chem. 2014 Sep 18. PMID:25230674[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Olaleye TO, Brannigan JA, Roberts SM, Leatherbarrow RJ, Wilkinson AJ, Tate EW. Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites. Org Biomol Chem. 2014 Sep 18. PMID:25230674 doi:http://dx.doi.org/10.1039/c4ob01669f
