4B12

Plasmodium vivax N-myristoyltransferase with a bound benzofuran inhibitor (compound 23)

Summary for 4B12

• Entry DOI: 10.2210/pdb4b12/pdb
• Related: 4A95 4B10 4B11 4B13 4B14
• Descriptor: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, 1-[3-methyl-4-(piperidin-4-yloxy)-1-benzofuran-2-yl]-3-phenylpropan-1-one, 2-oxopentadecyl-CoA, ... (8 entities in total)
• Functional Keywords: transferase, plasmodium, malaria, drug design
• Biological source: PLASMODIUM VIVAX
• Total number of polymer chains: 3
• Total formula weight: 140199.28

Authors

Yu, Z.,Brannigan, J.A.,Moss, D.K.,Brzozowski, A.M.,Wilkinson, A.J.,Holder, A.A.,Tate, E.W.,Leatherbarrow, R.J. (deposition date: 2012-07-06, release date: 2012-10-17, Last modification date: 2023-12-20)

Primary citation

Yu, Z.,Brannigan, J.A.,Moss, D.K.,Brzozowski, A.M.,Wilkinson, A.J.,Holder, A.A.,Tate, E.W.,Leatherbarrow, R.J.
Design and Synthesis of Inhibitors of Plasmodium Falciparum N-Myristoyltransferase, a Promising Target for Anti-Malarial Drug Discovery.
J.Med.Chem., 55:8879-, 2012

PubMed Abstract: Design of inhibitors for N-myristoyltransferase (NMT), an enzyme responsible for protein trafficking in Plasmodium falciparum , the most lethal species of parasites that cause malaria, is described. Chemistry-driven optimization of compound 1 from a focused NMT inhibitor library led to the identification of two early lead compounds 4 and 25, which showed good enzyme and cellular potency and excellent selectivity over human NMT. These molecules provide a valuable starting point for further development.

PubMed: 23035716
DOI: 10.1021/JM301160H

Experimental method

X-RAY DIFFRACTION (1.79 Å)