7QON の概要
| エントリーDOI | 10.2210/pdb7qon/pdb |
| 分子名称 | Triosephosphate isomerase, SODIUM ION, CHLORIDE ION, ... (6 entities in total) |
| 機能のキーワード | fasciolysis, isomerase |
| 由来する生物種 | Fasciola hepatica (liver fluke) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 112769.84 |
| 構造登録者 | |
| 主引用文献 | Kontellas, G.,Studholme, D.J.,van der Giezen, M.,Timson, D.J.,Littlechild, J.A.,Isupov, M.N. Triosephosphate isomerase from Fasciola hepatica: high-resolution crystal structure as a drug target. Acta Crystallogr.,Sect.F, 81:381-387, 2025 Cited by PubMed Abstract: The trematode liver fluke Fasciola hepatica causes the neglected tropical disease fascioliasis in humans and is associated with significant losses in agricultural industry due to reduced animal productivity. Triosephosphate isomerase (TPI) is a glycolytic enzyme that has been researched as a drug target for various parasites, including F. hepatica. The high-resolution crystal structure of F. hepatica TPI (FhTPI) has been solved at 1.51 Å resolution in its monoclinic form. The structure has been used to perform molecular-docking studies with the most successful fasciolocide triclabendazole (TCBZ), which has recently been suggested to target FhTPI. Two FhTPI residues, Lys50 and Asp51, are located at the dimer interface and are found in close proximity to the docked TCBZ. These residues are not conserved in mammalian hosts. PubMed: 40832834DOI: 10.1107/S2053230X25006454 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.51 Å) |
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