4A95

Plasmodium vivax N-myristoyltransferase with quinoline inhibitor

Summary for 4A95

• Entry DOI: 10.2210/pdb4a95/pdb
• Descriptor: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, 3-(3-BUTYL-6-METHOXY-2-METHYL-QUINOLIN-4-YL)SULFANYLPROPANENITRILE, 2-oxopentadecyl-CoA, ... (7 entities in total)
• Functional Keywords: transferase, malaria
• Biological source: PLASMODIUM VIVAX
• Total number of polymer chains: 3
• Total formula weight: 139033.63

Authors

Goncalves, V.,Brannigan, J.A.,Whalley, D.,Ansell, K.H.,Saxty, B.,Holder, A.A.,Wilkinson, A.J.,Tate, E.W.,Leatherbarrow, R.J. (deposition date: 2011-11-24, release date: 2012-06-27, Last modification date: 2024-05-01)

Primary citation

Goncalves, V.,Brannigan, J.A.,Whalley, D.,Ansell, K.H.,Saxty, B.,Holder, A.A.,Wilkinson, A.J.,Tate, E.W.,Leatherbarrow, R.J.
Discovery of Plasmodium Vivax N-Myristoyltransferase Inhibitors: Screening, Synthesis, and Structural Characterization of Their Binding Mode.
J.Med.Chem., 55:3578-, 2012

PubMed Abstract: 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.

PubMed: 22439843
DOI: 10.1021/JM300040P

Experimental method

X-RAY DIFFRACTION (1.55 Å)