4BBH

Plasmodium vivax N-myristoyltransferase with a bound benzothiophene inhibitor

4BBH の概要

• エントリーDOI: 10.2210/pdb4bbh/pdb
• 関連するPDBエントリー: 4A95 4B10 4B11 4B12 4B13 4B14
• 分子名称: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, DIMETHYL SULFOXIDE, 2-oxopentadecyl-CoA, ... (8 entities in total)
• 機能のキーワード: transferase, myristoylation, malaria, inhibitor
• 由来する生物種: PLASMODIUM VIVAX
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 139517.15

構造登録者

Rackham, M.D.,Brannigan, J.A.,Moss, D.K.,Yu, Z.,Wilkinson, A.J.,Holder, A.A.,Tate, E.W.,Leatherbarrow, R.J. (登録日: 2012-09-23, 公開日: 2012-12-05, 最終更新日: 2024-05-08)

主引用文献

Rackham, M.D.,Brannigan, J.A.,Moss, D.K.,Yu, Z.,Wilkinson, A.J.,Holder, A.A.,Tate, E.W.,Leatherbarrow, R.J.
Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium Falciparum and Plasmodium Vivax N-Myristoyltransferase.
J.Med.Chem., 56:371-, 2013

PubMed Abstract: N-Myristoyltransferase (NMT) is an attractive antiprotozoan drug target. A lead-hopping approach was utilized in the design and synthesis of novel benzo[b]thiophene-containing inhibitors of Plasmodium falciparum (Pf) and Plasmodium vivax (Pv) NMT. These inhibitors are selective against Homo sapiens NMT1 (HsNMT), have excellent ligand efficiency (LE), and display antiparasitic activity in vitro. The binding mode of this series was determined by crystallography and shows a novel binding mode for the benzothiophene ring.

PubMed: 23170970
DOI: 10.1021/JM301474T

実験手法

X-RAY DIFFRACTION (1.63 Å)