1TW9
Glutathione Transferase-2, apo form, from the nematode Heligmosomoides polygyrus
1TW9 の概要
| エントリーDOI | 10.2210/pdb1tw9/pdb |
| 分子名称 | glutathione S-transferase 2 (2 entities in total) |
| 機能のキーワード | transferase |
| 由来する生物種 | Heligmosomoides polygyrus |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 187334.62 |
| 構造登録者 | Schuller, D.J.,Liu, Q.,Kriksunov, I.A.,Campbell, A.M.,Barrett, J.,Brophy, P.M.,Hao, Q. (登録日: 2004-06-30, 公開日: 2004-08-03, 最終更新日: 2023-08-23) |
| 主引用文献 | Schuller, D.J.,Liu, Q.,Kriksunov, I.A.,Campbell, A.M.,Barrett, J.,Brophy, P.M.,Hao, Q. Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus. Proteins, 61:1024-1031, 2005 Cited by PubMed Abstract: The crystal structure of GST Nu2-2 (HpolGSTN2-2) from the model hookworm nematode Heligmosomoides polygyrus has been solved by the molecular replacement method and refined to a resolution of 1.71 A, providing the first structural data from a class of nematode-specific GSTs. By structural alignment with two Sigma class GSTs, glutathione could be rationally docked into the G-site of the enzyme. By comparing with all mammalian GST classes, a novel, long, and deep cleft was identified at the H-site, providing a potential site for ligand binding. This new GST class may support the establishment of infection parasitic nematodes by passively neutralizing chemical toxins derived from host environment. The structure serves as a starting point for structure-based drug/inhibitor design that would aim to selectively disrupt nematode chemical defenses. PubMed: 16189827DOI: 10.1002/prot.20649 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.71 Å) |
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