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

Year: 2024
Type: article
Abstract: 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 (PvNMT) 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 PvNMT 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 PvNMT as to human NMT.
DOI: 10.1107/s2053230x24011348
Authors: Alex Mendez, Cydni Bolling, Shane Taylor, Stanley Makumire, Bart Staker, Alexandra Reers, Brad Hammerson, Stephen J. Mayclin, Jan Abendroth, Donald D. Lorimer, Thomas E. Edwards, Edward W. Tate, Sandhya Subramanian, Andrew S. Bell, Peter J. Myler, Oluwatoyin A. Asojo, Graham Chakafana
Institutions: Hampton University, University of Oulu, Seattle Children's Research Institute, Center for Infectious Disease Research, Imperial College London, Dartmouth Cancer Center
Language: English
Field: Medicine
Open Access status: hybrid
Estimated APC paid: $3,350
OpenAlex ID: W4405206848
FWCI: 1.537
Cites: 44
Cited by: 4
Related to: 10