4C7H

Leismania major N-myristoyltransferase in complex with a peptidomimetic (-NH2) molecule

4C7H の概要

• エントリーDOI: 10.2210/pdb4c7h/pdb
• 関連するPDBエントリー: 4C68 4C7I
• 分子名称: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, MAGNESIUM ION, N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide, ... (8 entities in total)
• 機能のキーワード: transferase, myristoylation
• 由来する生物種: LEISHMANIA MAJOR
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50669.96

構造登録者

Olaleye, T.O.,Brannigan, J.A.,Goncalves, V.,Roberts, S.M.,Leatherbarrow, R.J.,Wilkinson, A.J.,Tate, E.W. (登録日: 2013-09-20, 公開日: 2014-09-24, 最終更新日: 2024-05-08)

主引用文献

Olaleye, T.O.,Brannigan, J.A.,Roberts, S.M.,Leatherbarrow, R.J.,Wilkinson, A.J.,Tate, E.W.
Peptidomimetic Inhibitors of N-Myristoyltransferase from Human Malaria and Leishmaniasis Parasites.
Org.Biomol.Chem., 12:8132-, 2014

PubMed Abstract: N-Myristoyltransferase (NMT) has been shown to be essential in Leishmania and subsequently validated as a drug target in Plasmodium. Herein, we discuss the use of antifungal NMT inhibitors as a basis for inhibitor development resulting in the first sub-micromolar peptidomimetic inhibitors of Plasmodium and Leishmania NMTs. High-resolution structures of these inhibitors with Plasmodium and Leishmania NMTs permit a comparative analysis of binding modes, and provide the first crystal structure evidence for a ternary NMT-Coenzyme A/myristoylated peptide product complex.

PubMed: 25230674
DOI: 10.1039/C4OB01669F

実験手法

X-RAY DIFFRACTION (1.4 Å)