5G22

Plasmodium vivax N-myristoyltransferase in complex with a quinoline inhibitor (compound 26)

5G22 の概要

• エントリーDOI: 10.2210/pdb5g22/pdb
• 関連するPDBエントリー: 5G1Z 5G20 5G21
• 分子名称: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, 2-oxopentadecyl-CoA, ETHYL 4-[(2-CYANOETHYL)SULFANYL]-6-{[6-(PIPERAZIN-1-YL), ... (7 entities in total)
• 機能のキーワード: transferase, myristoylation, malaria, inhibitor, quinoline, drug design
• 由来する生物種: PLASMODIUM VIVAX (MALARIA PARASITE P. VIVAX)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 139862.50

構造登録者

Goncalves, V.,Brannigan, J.A.,Laporte, A.,Bell, A.S.,Roberts, S.M.,Wilkinson, A.J.,Leatherbarrow, R.J.,Tate, E.W. (登録日: 2016-04-06, 公開日: 2017-02-15, 最終更新日: 2024-05-08)

主引用文献

Goncalves, V.,Brannigan, J.A.,Laporte, A.,Bell, A.S.,Roberts, S.M.,Wilkinson, A.J.,Leatherbarrow, R.J.,Tate, E.W.
Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.
Medchemcomm, 8:191-197, 2017

PubMed Abstract: The parasite is the most widely distributed cause of recurring malaria. -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 and -myristoyltransferase (NMT).

PubMed: 28626547
DOI: 10.1039/c6md00531d

実験手法

X-RAY DIFFRACTION (2.32 Å)