Structural highlights
Function
[A5K1A2_PLAVS] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586]
Publication Abstract from PubMed
N-Myristoyltransferase (NMT) is a prospective drug target against parasitic protozoa. Herein we report the successful discovery of a series of Plasmodium vivax NMT inhibitors by high-throughput screening. A high-resolution crystal structure of the hit compound in complex with NMT was obtained, allowing understanding of its novel binding mode. A set of analogues was designed and tested to define the chemical groups relevant for activity and selectivity.
Discovery of Plasmodium vivax N-myristoyltransferase inhibitors: screening, synthesis, and structural characterization of their binding mode.,Goncalves V, Brannigan JA, Whalley D, Ansell KH, Saxty B, Holder AA, Wilkinson AJ, Tate EW, Leatherbarrow RJ J Med Chem. 2012 Apr 12;55(7):3578-82. Epub 2012 Apr 3. PMID:22439843[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goncalves V, Brannigan JA, Whalley D, Ansell KH, Saxty B, Holder AA, Wilkinson AJ, Tate EW, Leatherbarrow RJ. Discovery of Plasmodium vivax N-myristoyltransferase inhibitors: screening, synthesis, and structural characterization of their binding mode. J Med Chem. 2012 Apr 12;55(7):3578-82. Epub 2012 Apr 3. PMID:22439843 doi:10.1021/jm300040p
