Structure-Guided Identification of Resistance Breaking Antimalarial N‑Myristoyltransferase Inhibitors

The attachment of myristate to the N-terminal glycine of certain proteins is largely a co-translational modification catalyzed by N-myristoyltransferase (NMT), and involved in protein membrane-localization. Pathogen NMT is a validated therapeutic target in numerous infectious diseases including mala...

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Veröffentlicht in:	Cell chemical biology 2019-07, Vol.26 (7), p.991-1000.e7
Hauptverfasser:	Schlott, Anja C, Mayclin, Stephen, Reers, Alexandra R, Coburn-Flynn, Olivia, Bell, Andrew S, Green, Judith, Knuepfer, Ellen, Charter, David, Bonnert, Roger, Campo, Brice, Burrows, Jeremy, Lyons-Abbott, Sally, Staker, Bart L, Chung, Chun-Wa, Myler, Peter J, Fidock, David A, Tate, Edward W, Holder, Anthony A
Format:	Artikel
Sprache:	eng
Schlagworte:	Acyltransferases - antagonists & inhibitors Acyltransferases - genetics Acyltransferases - metabolism Amino Acid Sequence antimalarial target Antimalarials - chemistry BASIC BIOLOGICAL SCIENCES crystal structure drug resistance development Enzyme Inhibitors - chemistry genetic manipulation Humans malaria Malaria, Falciparum - drug therapy myristoylation N-myristoyl Plasmodium Plasmodium falciparum - drug effects Plasmodium falciparum - metabolism Polymorphism, Single Nucleotide - genetics post-translational modification protein lipidation Protein Processing, Post-Translational transferase
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