Structure of Plasmodium vivax N -myristoyltransferase with inhibitor IMP-1088: exploring an NMT inhibitor for antimalarial therapy

• Published in: Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2025-01, Vol.81 (1)
• Main Authors: Mendez, Alex, Bolling, Cydni, Taylor, Shane, Makumire, Stanley, Staker, Bart, Reers, Alexandra, Hammerson, Brad, Mayclin, Stephen J., Abendroth, Jan, Lorimer, Donald D., Edwards, Thomas E., Tate, Edward W., Subramanian, Sandhya, Bell, Andrew S., Myler, Peter J., Asojo, Oluwatoyin A., Chakafana, Graham
• Format: Article
• Language: English
• ISSN: 2053-230X; 2053-230X
• DOI: 10.1107/S2053230X24011348

Plasmodium vivax , a significant contributor to global malaria cases, poses an escalating health burden on a substantial portion of the world's population. The increasing spread of P. vivax because of climate change underscores the development of new and rational drug-discovery approaches. The Seattle Structural Genomics Center for Infectious Diseases is taking a structure-based approach by investigating essential enzymes such as N -myristoyltransferase (NMT). P. vivax N -myristoyltransferase ( Pv NMT) is a promising target for the development of novel malaria treatments unlike current drugs, which target only the erythrocytic stages of the parasite. Here, the 1.8 Å resolution ternary structure of Pv NMT in complex with myristoyl-CoA and IMP-1088, a validated NMT inhibitor, is reported. IMP-1088 is a validated nonpeptidic inhibitor and a ternary complex structure with human NMT has previously been reported. IMP-1088 binds similarly to Pv NMT as to human NMT.