5g22: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A5K1A2_PLAVS A5K1A2_PLAVS]] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] | [[http://www.uniprot.org/uniprot/A5K1A2_PLAVS A5K1A2_PLAVS]] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] | ||
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== Publication Abstract from PubMed == | |||
The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT). | |||
Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.,Goncalves V, Brannigan JA, Laporte A, Bell AS, Roberts SM, Wilkinson AJ, Leatherbarrow RJ, Tate EW Medchemcomm. 2017 Jan 1;8(1):191-197. doi: 10.1039/c6md00531d. Epub 2016 Nov 11. PMID:28626547<ref>PMID:28626547</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
